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Biomedical subjects

M Kamo

Publications and source records attributed to M Kamo.

48 records · Page 3Linked to original sources
PubMed1992

Key factors to improve survival of elderly patients on CAPD.

The adequacy of dialysis is a primary concern when caring for patients undergoing CAPD. It is also important to analyze the key factors, which will reflect on the prognosis of elderly patients on CAPD. In this study, 60 CAPD patients were examined. The peritoneal and residual renal clearance of these patients were calculated every six months. These patients were divided into three groups (G-1 = poor, G-2 = fairly good, G-3 = good) according to their clinical parameter scores using a s-albumin,Ht,LBW, and s-cholesterol level. This study showed that the values of (KT/V) urea and Curea showed no statistical differences. These results therefore indicate that the major reason for the poor outcome in elderly patients is due to low dietary protein intake.

Aged↗
PubMed1990

Generation of a different type of beta-kallikrein from porcine pancreatic alpha-kallikrein by the action of chymotrypsin--observation of proteolytic processing occurring around "kallikrein autolysis loop" region.

The generation of a different type of beta-kallikrein, designated C beta-kallikrein, from alpha-kallikrein by chymotryptic action was ascertained by the following observations: 1) When alpha-kallikrein was incubated with chymotrypsin, an increase of esterolytic activity of kallikrein was observed. 2) In sodium dodecyl sulfate polyacrylamide gel electrophoresis, C beta-kallikrein was found to be different from the beta-kallikrein obtained from alpha-kallikrein by tryptic digestion, and was designated T beta-kallikrein. 3) N-Terminal amino acid sequence analyses of internal light and heavy chains of C beta-kallikrein indicated that N-termini of the light and the heavy chains were isoleucine and lysine, respectively, and that the heavy chain had most of the "kallikrein autolysis loop" sequence in its N-terminal end. In the case of T beta-kallikrein, N-termini of the light and the heavy chains were isoleucine and alanine, respectively, and the light chain retained the "kallikrein autolysis loop" region in its C-terminal end. These observations demonstrated that C beta-kallikrein was different from the beta-kallikrein prepared from autolyzed pancreas, A beta-kallikrein, which had lost the "kallikrein autolysis loop" sequence. Structural differences of the above four kallikreins (alpha-, T beta-, C beta-, and A beta-) result in somewhat different enzyme properties. The kinetic constants for the hydrolysis of synthetic substrates (N alpha-benzoyl-L-arginine ethyl ester and N alpha-tosyl-L-arginine methyl ester) of these kallikreins differed from each other, and inhibitory profiles against alpha 1-antitrypsin were also different.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1990

N-terminal amino acid sequence analysis of small subunits of photosystem I reaction center complex from a thermophilic cyanobacterium, Synechococcus elongatus Nägeli.

Four small subunits (14, 13, 10, and 8 kDa) of the photosystem I reaction center complex were isolated from a thermophilic cyanobacterium Synechococcus elongatus and their N-terminal amino acid sequences determined. Sequence analysis of the 10-kDa subunit revealed that the distribution of cysteine residues, Cys-X-X-Cys-X-X-Cys-X-X-X-Cys-Pro, is characteristic of bacterial-type ferredoxins, and that its partial sequence is highly homologous to that deduced from the chloroplast gene frx A of liverwort. This indicates that the 10-kDa polypeptide is an apoprotein carrying two iron-sulfur centers, FA and FB, assigned as [4Fe-4S] clusters, which mediated the light-activated transfer of electrons from P700 in photosystem I reaction center complex to soluble ferredoxin. The amino acid sequence of the 14-kDa polypeptide also showed similarity to that of the 20-kDa polypeptide from spinach chloroplast that can be chemically crosslinked with soluble ferredoxin. Thus, the 14-kDa polypeptide appears to be the ferredoxin 'docking' protein.

Amino Acid Sequence↗
PubMed1990

Hemerythrin from Lingula unguis consists of two different subunits, alpha and beta.

Hemerythrin, a non-heme Fe-protein, of Lingula unguis has an octamer structure. We demonstrated that the protein is composed of two distinct subunits (alpha and beta), in equal amounts by investigation of their composition and partial terminal sequence. The cross-linking reaction of the native protein with dithiobis-(succinimidyl propionate) provided evidence for the presence of a dimer composed of alpha and beta subunits.

Amino Acid Sequence↗
PubMed1989

Primary structure of spinach-chloroplast thioredoxin f. Protein sequencing and analysis of complete cDNA clones for spinach-chloroplast thioredoxin f.

The primary structure of thioredoxin f from spinach chloroplasts was determined by standard amino acid sequencing and furthermore by sequencing the corresponding nuclear genome region. The protein, with a calculated molecular mass of 12,564 Da and a molar absorption coefficient at 280 nm of 17,700 M-1 cm-1, consists of 113 residues and exhibits 24% residue identities with spinach chloroplast thioredoxin mb or Escherichia coli thioredoxin. A monospecific antibody elicited against thioredoxin f has been used to select recombinant phage from spinach cDNA libraries in lambda gt11. The inserts of positive clones were sequenced. They code for a polypeptide of 190 amino acids, composed of the thioredoxin f sequence (113 residues) and an upstream element (77 residues) which most probably constitutes the N-terminal transit peptide that directs the polypeptide into chloroplasts. In vitro transcription and translation of this construct generates a polypeptide of approximately 21 kDa, which is imported by isolated spinach chloroplasts and processed to the mature 12.5-kDa protein.

Amino Acid Sequence↗
PubMed1989

Sensitization of Edman amino acid derivatives using the fluorescent reagent, 4-aminofluorescein.

The ability to analyze amino acid derivatives at the femtomole level is one of the most interesting challenges in the field of protein microsequencing. 2-Anilino-5-thiazolinone amino acids, obtained by Edman degradation, were quantitatively derivatized with fluorescent primary amines. The most fluorescent reagent tested was 4-aminofluorescein. The amino acid derivatives sensitized with this reagent were separated using reversed-phase high-performance liquid chromatography and identified at the 100 attomole level. Incorporation of this method into the operation of a conventional automated sequencer is also described.

Amino Acid Sequence↗
PubMed1989

Amino acid sequence of ferredoxin isolated from Cyanidium caldarium strain RK-1.

Ferredoxin was isolated from ther eukaryotic alga Cyanidium caldarium strain RK-1 and its amino acid sequence was determined. The ferredoxin is composed of 97 amino acid residues, and its molecular weight is 10,599 excluding the iron-sulfur cluster. The amino acid sequence differs from that of C. caldarium strain 1355/1, by 24 amino acid substitutions plus one deletion at the amino terminus.

Amino Acid Sequence↗
PubMed1989

Amino acid sequences of ferredoxins from rice cultivars, japonica and indica.

Ferredoxins were isolated from the leaves of two rice cultivars, japonica and indica. The purified protein preparations each contained two components, the major (I) and the minor (II) ferredoxin. Ferredoxin I from each cultivars was sequenced. The amino acid sequences of the ferredoxin I from the two strains were found to be identical to each other. The sequence similarity with wheat ferredoxin is about 90%. Most of the amino acid alterations are located at the ends of the protein, with the sequences surrounding the iron-sulfur coordinating cysteine residues being well conserved.

Amino Acid Sequence↗
PubMed1988

Sensitization of amino acid derivatives obtained from Edman degradation with radioactively-labeled iodohistamine.

The minimum amount of proteins and peptides required for sequencing is constantly decreasing as more sensitive microsequencing methods are developed. The sensitization of and Edman degradation product is one such method. We took the 2-anilino 5-thiazolinone amino acid intermediates obtained from Edman degradation by conventional sequencing procedures, and quantitatively reacted them with a primary amine. The amine used was radioactive [125I]iodohistamine, which affords highly sensitive detection. The labeled amino acid derivatives were separated by thin layer chromatography. Ten femtomoles of a labeled derivative can be detected by autoradiography.

Amino Acids↗
PubMed1987

Carboxypeptidase digestion in the presence of detergents.

The detergents, sodium dodecyl sulfate (SDS), lauryl glutamate (LG), and octyl-(polydisperse)oligooxyethylene (Octyl-POE), were tested as to their effects on the activities of carboxypeptidases A, B, and P. In general, Octyl-POE showed little inhibition and SDS showed the strongest inhibition. Carboxypeptidase B was only slightly inhibited by SDS. The inhibitory effect of SDS on these enzyme activities depended not on its concentration but on its absolute amount. For a constant amount of SDS, the activities of carboxypeptidases A and B remained almost constant with increasing reaction volume. Commercial carboxypeptidase B is usually contaminated by carboxypeptidase A. With the addition of SDS, almost only carboxypeptidase B activity was detected.

Carboxypeptidases↗