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PubMed1979

The origin of nitrogen incorporated into compounds in the rumen bacteria of steers given protein- and urea-containing diets.

1. Two young Friesian steers fitted with rumen cannulas were each given three different isonitrogenous and isoenergetic diets for successive periods of 2-3 weeks. The diets consisted mainly of straw and tapioca, with the nitrogen supplied mainly as decorticated groundnut meal(DCGM; diet A), in approximately equal amounts of DCGM and urea (diet B), or entirely as urea (diet C). 2. At the end of each period on a given diet, part of the dietary urea of a morning feed was replaced by a solution of [15N]urea which was infused into the rumen. Samples of rumen contents were removed just before giving the 15N dose and at 1,3,5,7 and 24 h afterwards, concentrations of ammonia and its 15N enrichment were determined and samples of mixed bacteria were prepared. Amino acids, ammonia derived mainly from amide groups, and hexosamines were prepared by ion-exchange chromatography of acid-hydrolysates of the bacteria and analysed for 15N. 3. Approximate estimates of net bacterial N synthesis were made from turnover data for rumen fluid and 15N enrichments in rumen fractions. From the determined efficiency of incorporation of urea-N into bacteria recovered at the duodenum, it was calculated that on diets A, B and C respectively 82%, 37% and 0% of the bacterial N was derived from dietary protein or other non-urea sources. 4. [15N]urea was converted rapidly to ammonia and the 15N then incorporated into bacterial amide-N; it appeared at a slower rate in total bacterial non-amide-N. Rates of incorporation into non-amide-N were highest for glutamic acid, aspartic acid and alanine, and generally lowest for proline (pro), histidine (his), phenylalanine(phe), arginine(arg), methionine(met) and galactosamine. A similar ranking was also generally observed for relative 15N abundances (15N atoms % excess in N component divided by 15N atoms % excess in total bacterial N) achieved after several hours. Relative 15N abundances in his, arg and pro increased with decreasing protein (DCGM) in the diet but those in the other protein amino acids, including the poorly labelled met, phe (and its derivative tyrosine) did not. 5. It was concluded that different extents of labelling of the amino acids (at least those present mainly in protein) indicated that different amounts of preformed units (amino acids or peptides) were used. When an adequate supply of such units was available (particularly on diet A) pro, arg, his, met and phe were derived in this way to a greater extent than the other amino acids, but whereas synthesis of pro, arg and his increased on the low-protein diet C, that of met and phe did not. Thus met and phe may be limiting for bacterial growth on diets low in protein and high in non-protein-N. 6. Differences in the extent of labelling of other bacterial N components may be due to different turnover rates.

Amino Acids↗
PubMed2004

Endogenous amino acid flow in the avian ileum: quantification using three techniques.

The aim of the present study was to compare the protein-free diet, guanidinated casein (GuC) and enzyme hydrolysed casein (EHC) methods for the quantification of endogenous amino acid (AA) flow in the avian ileum. Growing broiler chickens (5 weeks old) were used. All three assay diets were based on dextrose, and in the GuC and EHC diets GuC or EHC were the sole source of N. Endogenous AA flows determined with the use of protein-free diet were considerably lower (P<0.05) than those determined by the GuC and EHC methods. The total endogenous AA flows determined by the GuC and EHC methods were almost 3-fold greater (P<0.05) than those determined by the protein-free diet. The endogenous AA values obtained from GuC and EHC methods were similar (P>0.05), except for the flow of arginine, which was lower (P<0.05) in the EHC method. Glutamic acid, aspartic acid, threonine and glycine were the predominant endogenous AA present in digesta from the distal ileum. The contents of methionine, histidine and cystine were lower compared with other AA. The method of determination had no effect on the AA composition of endogenous protein, except for threonine, glutamic acid, lysine, arginine and cystine. The concentrations of threonine and arginine were lower (P<0.05) and that of lysine was higher (P<0.05) with the EHC method compared with the other two methods. The concentration of glutamic acid was greater (P<0.05) and that of cystine was lower (P<0.05) in the EHC and GuC methods compared with the protein-free diet method. The results showed that the ileal endogenous flows of N and AA are markedly enhanced by the presence of protein and peptides, above those determined following feeding of a protein-free diet. It is concluded that the use of EHC and GuC methods enables the measurement of ileal endogenous losses in chickens under normal physiological conditions.

Amino Acids↗
PubMed1994

Comparative responses of genetically lean and fat chickens to lysine, arginine and non-essential amino acid supply. I. Growth and body composition.

1. Three experiments were performed to study the effects of amino acid imbalance on the growth of genetically lean (LL) or fat (FL) male chickens from 28 to 42 d of age. In experiment 1, five concentrations of digestible lysine were compared (4.75, 6.75, 7.75, 8.75 and 9.75 g/kg). In experiment 2, four concentrations of digestible arginine were compared (6.53, 7.69, 8.84 and 10.0 g/kg). In experiment 3, three diets were compared: a high-protein diet (189 g CP/kg), a low-protein diet containing added essential amino acids (EAA) (144 g CP/kg) and this low-protein diet supplemented with 40 g/kg of non-essential amino acids (NEAA) (glutamic acid+aspartic acid). 2. LL birds exhibited a lower growth rate than the FL when the diet was deficient in either lysine or arginine. Plotting weight gain against lysine or arginine intake suggested that most of this effect was caused by variations in food intake. 3. When protein gains (body or total proteins) were plotted against lysine or arginine intake, LL chickens appeared more efficient than FL chickens. 4. Similar growth rates, although slightly lower in FL, were obtained with low- and high-protein diets. However, NEAA supplementation of the low-protein diet reduced adiposity of LL and did not modify that of FL. Increasing crude protein content (all amino acids) was more effective than NEAA supplementation in decreasing the adiposity of both lines.

Amino Acids↗
PubMed1999

A comparison of ileal digesta and excreta analysis for the determination of amino acid digestibility in food ingredients for poultry.

1. The apparent ileal and excreta digestibilities of amino acids in 15 samples representing 12 food ingredients were determined using 5-week-old male broiler chickens. The ingredients included 3 samples of cereals (wheat, maize and sorghum), 6 samples of plant protein meals (soyabean meal, cottonseed meal, canola meal and sunflower meal) and 6 samples of animal protein meals (meat meal, meat-and-bone meal, feather meal and fish meal). 2. The test ingredients were incorporated as the sole source of dietary protein in assay diets. Each diet was offered ad libitum to 3 pens (4 birds/pen) from d 35 to d 42 post-hatching. Total collection of excreta was carried out during the last 4 d. All birds were killed on d 42 and the contents of the lower half of the ileum were collected. Apparent ileal and excreta amino acid digestibilities were calculated using acid-insoluble ash as the indigestible marker. 3. The influence of site of measurement was found to vary among food ingredients, among samples within an ingredient and among different amino acids within an ingredient. Ileal amino acid digestibility values were similar in some ingredients, but significantly lower or higher in others than the corresponding excreta values. 4. Average ileal and excreta amino acid digestibilities in sorghum and maize were similar, but significant differences were observed for individual amino acids. In contrast, ileal amino acid digestibility values were higher than the corresponding excreta digestibility values in wheat. 5. The average ileal and excreta digestibilites of amino acids in the 3 soyabean meal samples were similar although small, but significant differences were noted for individual amino acids. Site of measurement had no effect on the digestibility of amino acids in canola meal. Digestibilities of valine, isoleucine, phenylalanine, histidine, glutamic acid, alanine and tyrosine in sunflower meal and those of valine, methionine, isoleucine, leucine, lysine, glutamic acid and alanine in cottonseed meal were lower by excreta analysis. 6. Digestibilities in animal protein meals, with the exception of blood meal and fish meal, were consistently higher by excreta analysis. Ileal-excreta differences in individual amino acid digestibilities were more evident in feather meal, meat meal and meat-and-bone meal. 7. Threonine and valine were the indispensable amino acids that were more frequently influenced by the site of measurement. Of the dispensable amino acids, aspartic acid, serine, glutamic acid and alanine were the most affected. 8. Differences determined between ileal and excreta digestibilities in the present study clearly demonstrate that amino acid metabolism by hindgut microflora in chickens may be substantial and that digestibilities measured in the terminal ileum are more accurate measures of amino acid availability than those measured in the excreta.

Amino Acids↗
PubMedDate not supplied

The amino acid composition of the proteinaceous component of guar gum (Cyamopsis tetragonolobus).

Guar gum, powdered endosperm from the seeds of the legume Cyamopsis tetragonolobus, is a galactomannan which contains 2.5-4.5% of a proteinaceous component. Data presented for 11 bulk commercial samples show that the most abundant amino acids are glycine, glutamic acid, aspartic acid, serine and alanine, but that their relative proportions vary considerably. The proportions of other amino acids, e.g. histidine, isoleucine, phenylalanine, threonine, tyrosine and valine are remarkably constant. There appear to be some correlations between viscosity and the glycine, arginine and proline contents. Data for the amino acid compositions of several chemical derivatives of a medium-viscosity gum guar sample indicate that the proteinaceous component is retained but suffers variable modification. The amino acid profile for guar gum differs extensively from those for gum arabic and gum karaya; this provides a useful analytical supplement to sugar determinations for studies of admixtures of these hydrocolloids.

Amino Acids↗
PubMed1987

[Utilization of 15N-labeled urea in laying hens. 8. 15N-incorporation in the amino acids of the oviduct].

3 colostomized laying hybrids received orally with a conventional ration 1% urea with 96.06 atom-% 15N excess (15N'). over a period of 6 days. In the period of the experiment every hen consumed 2.87 g 15N'. After another 2 days, on which they received conventional feed urea, the animals were butchered. 15N' was determined in the total N and in 15 amino acids of the oviduct. Of the 15 amino acids the labelling of glutamic acid, glycine and serine was highest and on average amounted to 0.80, 0.66 and 0.67 atom-% 15N'. In lysine and arginine only 0.10 and 0.11 atom-% 15N' could be detected. The amino acid N with natural isotopic frequency amounted to a quarter for the basic amino acids, a tenth for the branched chain ones and for the non-essential ones (glutamic acid, aspartic acid, serine, glycine, alanine, proline) a third of the total oviduct 14N, The average quota of 15N' is only 3.6%, that of the branched chain amino acids 4.5 and that of the non-essential ones 21.1%. Consequently, the 15N' of the urea is mainly used for the synthesis of the non-essential amino acids of the oviduct.

Amino Acids↗
PubMed1955

On the chemical composition of the axoplasm of squid giant nerve fibers with particular reference to its ion pattern.

Investigations dealing with the determination of the major chemical constituents of the axoplasm of the giant nerve fiber of the squid are described. Particular emphasis has been placed on determining the components involved in acid-base balance. It was found that 72 per cent of the total solids of axoplasm, representing 13.5 per cent of the wet material, are of relatively low molecular weight (dialyzable) and consist mainly of charged ionic or dipolar constituents. Of the 520 micromoles per gm. of total base, 72 per cent are balanced by organic acids: aspartic acid (65 micro equivalents per gm.), glutamic acid (10 micro equivalents), fumaric and succinic acids (15 micro equivalents), a new polycarboxylic acid (35 micro equivalents), and isethionic acid, a biologically novel sulfonic acid (220 micro equivalents). Besides potassium, sodium, small amounts of calcium, and magnesium there is a considerable fraction of organic (nitrogenous) base. Other features of the chemical composition of squid axoplasm include a relatively high concentration of taurine (100 micro equivalents) and an ultraviolet absorbing substance possibly identical with N-methylpicolinic acid. The distribution of the phosphates, especially the concentration of ATP, has been investigated. Specific techniques elaborated in connection with this study have been described and the biochemical implications of the analytical results are discussed.

Acid-Base Equilibrium↗
PubMed1958

Latent viral infection of cells in tissue culture. VI. Role of amino acids, glutamine, and glucose in psittacosis virus propagation in L cells.

Mouse fibroblasts (L cells) fail to support the growth of psittacosis virus (6BC strain) if they are maintained on a medium containing only inorganic salts and glucose for 2 days prior to infection. Virus propagation can be stimulated by the addition of a synthetic medium containing amino acids, water-soluble vitamins, glutamine, glucose, and inorganic salts. By omitting single amino acids from the complete synthetic medium, tyrosine, threonine, methionine, isoleucine, phenylalanine, tryptophan, leucine, valine, and cysteine or cystine were found to be essential for stimulation, while lysine, arginine, histidine, hydroxyproline, proline, glutamic acid, aspartic acid, serine, alanine, and glycine were not essential. The cells on deficient media showed varying degrees of degenerative changes, but there was little correlation between ability to support psittacosis virus growth and morphologic condition of the cells. Glucose is also an essential component of the medium for viral growth, but the absence of glutamine had no effect on stimulation of virus propagation. L cell cultures maintained on media deficient in phenylalanine or tryptophan for 2 days before infection were also found to be incapable of supporting virus growth. The implications of this study in latent viral infections are discussed.

Amino Acids↗
PubMed1962

Isolation and properties of a surface antigen of Staphylococcus aureus.

A technique is described for the isolation and purification of an antigen released into the culture medium by Staphylococcus aureus strain Smith. The antigen was found to be homogeneous when examined by free electrophoresis and analytic ultracentrifugation. Immunologic homogeneity was established by immunoelectrophoresis and quantitative precipitin tests using high titer antiserum prepared against the homologous organism. Chemical analysis showed that the antigen contained 70 per cent carbohydrate, of which approximately 30 to 35 per cent was believed to be glucosamine. The analytic data suggested that another amino sugar, probably carboxylated, was also present, but extreme lability of this compound to mild hydrolytic procedures has thus far precluded further identification. The remainder of the antigen was composed of alanine, glutamic acid, aspartic acid, lysine, glycine, serine, and threonine. No muramic acid was found. The chemical and physical data indicate that the antigen described herein is a previously unrecognized component of Staphylococcus aureus. The purified compound was capable of absorbing agglutinating antibody from antiserum prepared against S. aureus Smith, indicating that it was a surface component of this encapsulated staphylococcus. It is proposed that the antigen be known as the Smith surface antigen (SSA). The injection of SSA into rabbits did not produce precipitating antibodies. However, SSA did precipitate at low concentrations (0.5 microg/ml) with antiserum prepared against S. aureus Smith and one other strain of S. aureus tested. Antiserum against two other aureus strains reacted only with high concentrations of SSA. SSA did not react with S. albus antiserum or with normal sera from several animal species. Experiments are in progress to define further the distribution of SSA. Intradermal injection of small quantities of SSA into rabbits immunized with S. aureus Smith evoked a reaction of cutaneous hypersensitivity, which was maximal in 8 to 12 hours. SSA appeared to be the substance responsible for the ability of S. aureus Smith to resist engulfment by phagocytes, since absorption of Smith antiserum with SSA effectively removed opsonizing antibodies. SSA induced protection in mice against experimental staphylococcal disease. The subcutaneous injection of 0.1 microg resulted in protection against a subsequent intraperitoneal challenge with 50 to 100 LD(50)'s of S. aureus Smith suspended in mucin. Increasing as well as decreasing the immunizing dose resulted in significantly less protection.

Animals↗
PubMed1996

TCR binding differs for a bacterial superantigen (SEE) and a viral superantigen (Mtv-9).

Both superantigens (SAG) and many anti-TCR monoclonal antibodies (mAb) have specificity for the V beta region of the TCR encoded by TCRBV genes. For instance the bacterial SAG staphylococcal enterotoxin E (SEE), the retroviral SAG MTV-9 and the mAb OT145 each react with human T cells expressing BV6S7. This BV gene encodes two common alleles. We found that SEE and the mAb preferentially activate T cells expressing BV6S7*1 as opposed to BV6S7*2, but Mtv-9 activates T cells expressing either allele. Thus binding to the TCR differs between the two SAGs. A mutation in the TCR HVR-4 region of BV6S7*1 (G72E), where the two BV6S7 alleles differ, indicated that HVR-4 is a component of the binding site for SEE and for the mAb OT145. BV6S7*2 has a charged E72 which may result in electrostatic repulsion of SEE, as SEE contains a similarly acidic aspartic acid residue at a TCR interaction site (204D).

Alleles↗
PubMed1984

Massive cutaneous hyalinosis. Identification of the hyalin material as monoclonal kappa light chains, adhesive 90 kD glycoprotein, and type I collagen.

The hyalin material in massive cutaneous hyalinosis, a disease characterized by extensive tumorous periodic acid-Schiff-(PAS) positive extracellular cutaneous deposits, has been elucidated by biochemical and immunologic methods. Three major components were found: kappa light chains, a mannose-rich glycoprotein, and type I collagen. Trace amounts of fibrinogen, fibronectin, laminin, IgG, pregnancy-specific glycoprotein, albumin, and keratan sulfate, but not keratin, were also present. The kappa light chains were monoclonal, cryoprecipiting, and more basic than the kappa chains from two myeloma patients. The glycoprotein, which could not be identified as any known glycoprotein, had an apparent molecular weight of 90,000 D. Amino acid analysis showed that glutamic acid, aspartic acid, leucine, and threonine were abundant, whereas hydroxyproline, hydroxylysine, and sulfhydryl amino acids were absent. The carbohydrate content of the protein was approximately 20%. The major monosaccharides were mannose and N-acetylglucosamine. Galactose, N-acetylneuraminic acid and fucose also were present. The third major component of the hyalin material was identified as type I collagen. A humoral immune response to the storage material was found: the patient's serum contained IgM and IgG class antibodies against the mannosylglycoprotein (90 kD glycoprotein) and against type I collagen.

Aged↗
PubMed1992

Evidence for a ras gene mutation in azoxymethane-induced colonic aberrant crypts in Sprague-Dawley rats: earliest recognizable precursor lesions of experimental colon cancer.

The main objective of the present investigation was to understand the molecular events involved in the genesis of aberrant crypt foci. Aberrant crypt foci were induced in Sprague-Dawley rats with a single injection of azoxymethane. Aberrant crypts have been identified topographically in the colon and are hypothesized to represent preneoplastic lesions. In order to understand the molecular events involved in the early stages of colon cancer, PCR-amplified DNA from aberrant crypts was hybridized with oligonucleotide probes specific for the detection of point mutations in codon 12 of K-ras. The mutation identified was a G to A transition resulting in the substitution of the amino acid aspartic acid (asp) for glycine (gly). This mutation was present in 6/19 (32%) of aberrant crypts examined. The identical mutation was also identified in adenomacarcinoma tissue while no mutation could be detected in normal intestinal mucosa. For further confirmation of these results, the presence of the mutated ras protein (rasAsp-12) was detected in aberrant crypts by immunohistochemistry. This investigation provides the first identification of a ras point mutation in aberrant crypt foci.

Adenocarcinoma↗
PubMed2000

Capillary electrophoresis for the determination of major amino acids and sugars in foliage: application to the nitrogen nutrition of Sclerophyllous species.

Amino acids and sugars are probably the most commonly measured solutes in plant fluids and tissue extracts. Chromatographic techniques used for the measurement of such solutes require complex derivatization procedures, analysis times are long and separate analyses are required for sugars and amino acids. Two methods were developed for the analysis of underivatized sugars and amino acids by capillary electrophoresis (CE). Separation of a range of sugars and amino acids was achieved in under 30 min, with good reproducibility and linearity. In general, there was close agreement between amino acid analyses by CE and HPLC with post-column derivatization. An alternative, more rapid method was optimized for the common neutral sugars. Separation of a mixture of fructose, glucose, sucrose, and fucose (internal standard) was achieved in less than 5 min. How the source of N applied (nitrate or ammonium) and its concentration (8.0 or 0.5 mM) affects the amino acid and sugar composition of leaves from Banksia grandis Willd. and Hakea prostrata R. Br. was investigated. The amino acid pool of Banksia and Hakea were dominated by seven amino acids (aspartic acid, glutamic acid, asparagine, glutamine, serine, proline, and arginine). Of these, asparagaine and glutamine dominated at low N-supply, whereas at high N-supply the concentration of arginine increased and dominated amino-N. Plants grown with nitrate had a greater concentration of proline relative to plants with ammonium. In Banksia the concentration of amides was greatest and arginine least with a nitrate N-source, whereas in Hakea amides were least and arginine greatest with nitrate N-source. The concentration of sugars was greater in Banksia than Hakea and in both species at greater N-supply.

Amino Acids↗
PubMed1992

Essential histidine residue in 3-ketosteroid-delta 1-dehydrogenase.

The variation with pH of kinetic parameters was examined for 3-ketosteroid-delta 1-dehydrogenase from Nocardia corallina. The Vmax/Km profile for 4-androstenedione indicates that activity is lost upon protonation of a cationic acid-type group with a pK value of 7.7. The enzyme was inactivated by diethylpyrocarbonate at pH 7.4 and the inactivation was substantially prevented by androstadienedione. Analyses of reactivation with neutral hydroxylamine, pH variation, and spectral changes of the inactivated enzyme revealed that the inactivation arises from modification of a histidine residue. Studies with [14C]diethylpyrocarbonate provided support for the idea that the 1-2 essential histidine residues are essential for the catalytic activity of the enzyme. Dye-sensitized photooxidation led to 50% inactivation of the enzyme with the decomposition of two histidine residues. This inactivation was also prevented by androstadienedione. Dancyl chloride caused a loss of the enzyme activity. Modifiers of glutamic acid, aspartic acid, cysteine, and lysine did not affect the enzyme activity. Butanedione and phenylglyoxal in the presence of borate rapidly inactivated the enzyme, indicating that arginine residues also have a crucial function in the active site. The data described support the previously proposed mechanism of beta-oxidation of 3-ketosteroid.

Binding Sites↗
PubMed1978

Isolation and characterization of proteoheparan sulfate from plasma membranes of an ascites hepatoma, AH 66.

A proteoglycan was isolated from plasma membranes prepared from AH 66 cells by the following procedure. The plasma membranes were isolated from cells according to the method devised by Funakoshi and Yamashina (1976) J. Biochem. 80, 1185-1193), then the membranes were made lipid-free. The lipid-free membranes were solubilized with 5 mM sodium phosphate buffer, pH 7.0, containing 0.5% sodium dodecyl sulfate (SDS), then the solution was fractionated on a Sepharose CL 6B column. The proteoglycan eluted near the void volume fraction was further purified by repeated precipitation with cetylpyridinium chloride (CPC). The proteoglycan isolated was homogeneous on electrophoresis on a cellulose acetate strip and was identified as proteoheparan sulfate. The preparation contained 10.6% protein, its amino acid composition being characterized by high contents of glutamic acid, aspartic acid, proline, glycine, threonine, and serine.

Amino Acids↗
PubMed1997

High-resolution crystal structure of M-protease: phylogeny aided analysis of the high-alkaline adaptation mechanism.

M-protease is a subtilisin-family serine protease produced by an alkaliphilic Bacillus sp. strain. Optimal enzymatic activity of the protein occurs at pH 12.3. The crystal structure of M-protease (space group P2(1)2(1)2(1), a = 62.3, b = 75.5, c = 47.2 A) has been refined to a crystallographic R-factor of 17.2% at 1.5 A resolution. The alkaline adaptation mechanism of the enzyme was analyzed. Molecular phylogeny construction was used to determine the amino acid substitutions that occurred during the high-alkaline adaptation process. This analysis revealed a decrease in the number of negatively charged amino acids (aspartic acid and glutamic acid) and lysine residues and an increase in arginine and neutral hydrophilic amino acids (histidine, asparagine and glutamine) residues during the course of adaptation. These substitutions increased the isoelectric point of M-protease. Some of the acquired arginine residues form hydrogen bonds or ion pairs to combine both N- and C-terminal regions of M-protease. The substituted residues are localized to a hemisphere of the globular protein molecule where positional shifts of peptide segments, relative to those of the less alkaliphilic subtilisin Carlsberg, are observed. The biased distribution and interactions caused by the substituted residues seem to be responsible for stabilization of the conformation in a high-alkaline condition.

Adaptation, Physiological↗
PubMed1998

Transamination of 2-oxo-4-[methylthio]butanoic acid in chicken tissues.

The keto acid 2-oxo-4[methylthio]butanoic acid (OMTB) is an intermediate in the conversion of synthetic feed grade methionine sources to L-methionine in vivo in poultry and other animals. Because methionine sources are utilized by the chick with considerably less than 100% efficiency as sources of L-methionine, it is important to determine what metabolic process may limit the utilization of these sources. Because OMTB is converted to L-methionine by transamination, a study was conducted to determine which amino acids might serve as nitrogen donors in the conversion of OMTB to L-methionine in the chicken. Dialyzed tissue homogenates, mitochondria, and cytosol from liver, kidney, intestine, and skeletal muscle were incubated with OMTB and individual L-amino acids (isoleucine, leucine, valine, glutamic acid, aspartic acid, alanine, glutamine, asparagine, and phenylalanine) and the methionine that accumulated was determined by ion exchange chromatography. Tissues differed in the conversion of OMTB to methionine: kidney was most active, liver and intestinal mucosa were intermediate, and skeletal muscle had lowest activity. All amino acids supported methionine synthesis. Branched-chain amino acids and glutamic acid were the most effective substrates in tissue cytosols except in intestinal mucosa, in which asparagine was also effective. The preferred substrates in mitochondria were glutamate in liver mitochondria, isoleucine and alanine in kidney mitochondria, and branched-chain amino acids and glutamic acid in skeletal muscle mitochondria. All amino acids except alanine supported methionine synthesis from OMTB in mitochondria of intestinal mucosa. We conclude that a wide variety of amino acids can serve as substrates for transamination of OMTB in the chicken, and that the availability of nitrogen donors is unlikely to be a limiting factor in the conversion of OMTB to methionine.

Amino Acids↗
PubMed2000

Autosomal albino chicken mutation (ca/ca) deletes hexanucleotide (-deltaGACTGG817) at a copper-binding site of the tyrosinase gene.

We compared tyrosinase cDNA sequences from a line of autosomal albino and Black Silky chickens isolated from cultured melanocytes by reverse transcription-polymerase chain reaction (RT-PCR). Both sources produce a single DNA fragment of predicted normal tyrosinase size. Direct sequencing of the PCR product showed three mutated sites in the tyrosinase gene of the albino chicken. Two silent point mutations and a deletion of six nucleotides (-deltaGACTGG) at 817 bp in the tyrosinase cDNA sequence were observed when compared with the White Leghorn and Black Silky cDNA sequences. The deduced albino chicken tyrosinase protein lacks two amino acids, aspartic acid and tryptophan. The position of these amino acids is consistent with one of the potential copper-binding sites that should be indispensable for function of the enzyme. We speculate that the six-base deletion is responsible for the inactive tyrosinase in this line of albino chickens.

Amino Acid Sequence↗