[Pneumococcal meningitis in children].
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Child↗
Biomedical subjects
R Noack
Publications and source records attributed to R Noack.
[Physiological importance of microvilli-bound leucine arylamidase in the final digestion of proteins. 1. Purification and isolation of intestinal leucine arylamidase and aminotripeptidase of rats].
The membrane-bound leucine arylamidase of the microvilli of the rat small intestine was solubilized by Triton X-100 and purified by gel and ion-exchange chromatography. As compared to the mucosa homogenate, the purification factor was 135. The leucine arylamidase and aminotripeptidase of the microvilli cannot be separated by chromatography. The cytosomal portion of the aminopeptidase is devoid of leucine arylamidase activity.
Aminopeptidases↗
[Pathogenesis, clinical aspects and realistic risk factors in obesity].
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Adipose Tissue↗
The hypolipaemic action of a glycine rich diet in rats.
Feeding of a glycerine rich diet with sufficient supply of essential amino acids (mixture of casein and gelatine) causes a significant reduction of the serum triglyceride level in rats. To study some aspects of this triglyceride lowering effect the in vivo incorporation of C14-1-acetate and C14-1-palmitate into the serum and liver lipids as well as the lipoprotein lipase and the hormone sensitive lipolytic activity of the epididymal adipose tissue in vitro were estimated. After feeding the gelatine containing diet the incorporation of labelled acetate and palmitate into the serum triglycerides was significantly decreased with no change of the incorporation into the liver triglycerides and without detectable accumulation of liver lipids. The decreased serum triglyceride level of the serum corresponded to a decreased lipoprotein lipase activity in the epididymal adipose tissue, whereas the basal and norepinephrine stimulated lipolysis of this tissue was not affected. From these results it is concluded that due to feeding of a glycine rich diet the triglyceride secretion of the liver is decreased leading to a lower serum triglyceride level.
Acetates↗
[Physiological importance of the microvilli-bound leucine arylamidase in the final digestion of proteins. III. Exopeptidatic activities of purified microvilli against peptides mixtures in the presence and after the removal of free amino acids].
The exopeptidatic degradation of peptide mixtures by the aminopeptidase of the microvilli is inhibited by the presence of free amino acids. Further degradation occurs after the removal of the free amino acids from the peptide mixture. The amino-acid composition of the remaining residual peptides is a second factor that impedes the complete cleavage of the peptides.
Amino Acids↗
[Nutritional-physiological studies on acetylated fractions of protein from Vicia faba].
The nutritional-physiological value of an easily soluble and of a difficulty soluble fraction of protein from Vicia faba (showing a degree of acetylation of 0%, 43% and 94%, respectively) was characterized by determining the amino-acid content, the enzymatic amino-acid availability and the nitrogen balance in the rat. The results from both the amino-acid analysis and the animal experiments on the biological value evidenced that the nutritional-physiological value of the easily soluble fraction of protein from Vicia faba is significantly lower, which is in particular attributable to its lower content of sulphur-containing amino acids. Acetylation did not reduce the nutritional-physiological value of the easily soluble fraction of protein from Vicia faba, and impaired that of the difficulty soluble fraction but slightly. From the viewpoint of nutritional physiology, there are no objections against the use of these protein fractions as food additives.
Acetylation↗
[Physiological importance of microvilli-bound leucinarylamidase in the final digestion of proteins. 4. Inhibition of microvilli-bound leucinarylamidase by free amino acids].
The microvilli-bound leucine arylamidase is inhibited by certain amino acids. An inhibitory action is exerted by the branched-chain amino acids L-leucine and L-isoleucine and by the aromatic amino acids L-tyrosine and L-phenylalanine with Ki values of 4--6 . 10(-3) M. L-methionine (Ki = 2.5 . 10(-3) M) and its higher homologue L-ethionine (Ki = 1.1 . 10(-3) M) are the most potent inhibitors. Derivatization of L-methionine on the sulphur or the nitrogen atom or the carboxyl group prevents the inhibitory effect just as the D-isomer.
Amino Acids↗
[Spontaneous solubilization of mcuosal peptide hydrolases in rat small intestine].
In vitro incubations of small intestine preparation lead to the spontaneous release of mucosal enzymes into the incubation medium, due to superficial dissolution and membrane lesions. One-hour anaerobic incubation of everted small intestine segments produces the liberation of from 13% (leucine arylamidase) to 30% (Gly-L-Pro-splitting peptide hydrolase) of the mucosal enzyme activities. Under the conditions of in vivo perfusion, the solubilization rates are from 50 to 80% lower than these values. The tendency to solubilization is only in part reduced to a significant extent by the saturation of the incubation medium with oxygen, but it does not reach the in vivo level. The detectability of membrane-bound and intracellular marker enzymes in the incubation medium permits no conclusions concerning the physiological localization of the released peptidases.
Anaerobiosis↗
[Absorption of triglycine, diglycine, glycine or equimolar mixtures of diglycine and glycine in the perfused small intestine of rats].
1. After a wash-out period of 20 min with Krebs-Henseleit-buffer a 20 cm segment of proximal or distal small intestine of nonanaesthesized rats got a bolus infusion of 3 ml either triglycine, diglycine, glycine or an equimolar mixture of diglycine and glycine, respectively, in a concentration range of 20 to 1000 mmol/l glycine equivalents. With 9 ml of a peptide and amino acid free solution the gut was perfused in a single-pass perfusion and the whole fluid recovered was investigated by quantitative thin layer chromatography for triglycine, diglycine and glycine. 2. In the concentration range up to 170 mmol/l glycine equivalents the nitrogen absorption is independent of the substrates perfused. In the highest concentration range an additional increased disappearance of triglycine could be found. This change cannot be observed to the same extent for diglycine, glycine or the mixture of both. In contrast, in the highest concentration range the competition between glycine and diglycine results in a decrease of absorption. 3. The proximal or distal nitrogen absorption of all substrates is similar. 4. In the perfusate the peptide and its splitting products were investigated. 5. Based on the discrepancy between the disappearance of triglycine and the appearance of its splitting products it is assumed. 1. that the transport of intact triglycine is of quantitative importance in the highest concentration range and 2. that in the lower concentration range membrane digestion followed the transport of the splitting products prevails. 6. Extending Ugoley's model for dipeptides three general variations for membrane digestion of tripeptides are proposed. One of this is likely for the triglycine absorption.
Animals↗
The influence of postnatal nutrition on lipoprotein lipase activity and hormone sensitive lipolysis in vitro of rat adipose tissue.
In rats grown up in small and large nests the lipolytic activity of adipose tissue was studied in vitro in dependence on age. Independent of age and sex a significantly higher lipoprotein lipase activity as well as a lower basal or norepinephrine stimulated lipolysis and reesterification (absolute) occurred in rats from small nests compared with rats from large nests. The calculated degree of reesterification was independent of the nest size, but decreased from 80% to 30% from one month to one year of age. The marked differences in the lipolytic activities of adipose tissue emphasize the distinct influence of the post-natal nutrition on metabolic functions in the later life and lead to the conclusion that the metabolism of adipose tissue of animals from small nests is directed towards a long-term increased storage of lipids.
Adipose Tissue↗
[Amino acid composition of non-absorbed peptide fractions in rat small intestines. III. Feeding of wheat gluten and molasses yeast. Essential amino acid content of feces].
The authors investigated the nitrogen content of different fractions and in particular the aminoacid composition of the trichloroacetic acid (TCA)-precipitable and TCA-soluble peptides in the distal small intestine of rats which had been fed experimental diets (nitrogen-free or containing casein, wheat gluten or molasses yeast as a protein carrier). Parallel with this, they determined in growing rats the nitrogen and amino-acid digestibility of molasses yeast and wheat gluten according to the technique of faecal analysis, and studied the amino-acid composition of the faecal protein. Independently of the dietary protein fed, the peptide fractions of the content of the intestine showed an amino-acid composition that was largely similar to that found in case of nitrogen-free diet. The amino-acid composition of the faecal protein is, independently of the dietary protein given, relatively constant and corresponds approximately to the intestinal loss protein. There is agreement between the amino-acid composition of the TCA-precipitable peptide fractions and those of the corresponding faecal proteins. These components seem to be of endogenous origin.
Amino Acids↗
[Inhibition of aminopeptidase activity of rat small intestine by the tripeptide H-Thr-(O-tert. butyl)-Phe-Pro-OH].
The hydrolysis of L-leucine-beta-naphthylamide and L-leucinamide by leucinaminopeptidase (E.C. 3.4.11.1) from bovine eye lens is inhibited by H-Thr (O-tert. butyl)-Phe-Pro-OH. The inhibitor constants are Ki = 1.5 . 10(-5) M and 0.8 . 10(-5) M, respectively. Both brush border peptidases, leucinarylamidase (E.C. 3.4.11.2) AND TRIPEPTIDASE (E.C. 3.4.11.4), are inhibited to a smaller extent (Ki = 0.8 . 10(-3) M). Mn++-ions activate the cytosolic leucinaminopeptidase but not the hydrolysis of leucinamide by the brush border arylamidase. The inhibition of the cytosolic leucinamidase by the peptide (Ki = 3.5 . 10(-4)) is twice as that of the brush border arylamidase.
Aminopeptidases↗
[Nutritive-physiological study of sunflower seed protein isolate and spun sunflower seed protein-casein fibers].
Compared with defatted sunflower seeds, in sunflower seed globulin isolates the content of lysine and sulphur containing amino acids is decreased, the content of phenylalanine is increased. The content of the whole essential amino acids of sunflower seed globulin isolate in relation to casein is decreased. The value of the enzymatic invitro available amino acids of sunflower seed globulin is comparable with casein. The digestibility is good, the biological value is in relation to defatted sunflower seed lower. Apart from the lower content of sulphur-containing amino acids the amino acid composition of spun sunflower seed globulin/casein (I:I) fibers corresponds with the calculated value; in relation to sunflower seed globulin isolate the content of lysine and the whole essential amino acids of the spun protein fibers is increased. The enzymatic in-vitro-hydrolysis results altogether in a comparable availability of the amino acids between spun protein fibers and sunflower seed globulin isolates. The digestibility and the biological value of spun protein fibers corresponds with that of casein.
Amino Acids↗
Variation of the nutritive value of proteins by processing textured proteins.
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Aldehydes↗
[In vivo resorption of trypsin- and thermitase-cleaved casein and analogous amino acid mixtures].
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Amino Acids↗
[Amino acid composition of unresorbed peptide fractions in the contents of the distal part of rat small intestine. 1. Nitrogen-free diet and diets with casein, sunflower protein isolate and defatted sunflower seeds].
After feeding with protein containing diets the protein quantity increases in the aqueous supernatant (U1), in the trichloracetic acid soluble (U2) and precipitable (S2) fractions of the content of the distal part of the small intestine of rats. Independent of the dietary proteins the amino acid composition of both fractions (S2 and the peptides from U2) is similar in relation to protein-free feeding; a similarity with the amino acid composition of the dietary proteins doesn't exist. In relation to fraction S2 the peptides of fraction U2 show anording to the higher content of amino acids, which are difficult to liberate by protein cleavage, a high proteolytic degradation.
Amino Acids↗
Regulation of body temperature.
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Body Temperature Regulation↗
[Amino acid composition of the unresorbed peptide fractions of the distal part of the small intestine in rats. II. Feeding of field-bean protein isolate with and without the addition of dialdehyde starch and of protein texturates from it].
Rats were fed diets containing 20% protein in the form of casein, protein isolate from sunflower seeds, protein isolate from field beans, model protein texturate made from field-bean protein isolate or model protein texturate made from field-bean protein isolate treated with dialdehyde starch and a nitrogenfree diet. The content in the distal small intestine of the rats was collected 3 hours after feeding, and the amino-acid compositions of the TCA-precipitable and TCA-soluble peptides (after separation of free amino acids) of the content were studied. The comparison of the amino-acid compositions of the two peptide fractions with the respective dietary protein showed no agreement. On the contrary, the comparison of the amino-acid compositions of the two peptide fractions determined after protein-free diet with those found after protein ingestion were in good agreement, independently of the kind of dietary protein. The comparison of the two peptide fractions with one another revealed an increased degree of proteolytic decomposition of the TCA-soluble peptides. As compared to the other protein-containing diets and to the protein-free diet, diets containing field-bean protein caused an increase of TCA-precipitable peptides and an increase of glycine in both fractions. This was also observed in model protein texturates containing only 30% field-bean protein. Treatment with dialdehyde starch produces certain alterations of the basic amino acids and their accumulation in the fractions of undigested peptide.
Aldehydes↗