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Biomedical subjects

G Matsuda

Publications and source records attributed to G Matsuda.

At least 55 records · Page 3Linked to original sources
PubMed1985

Amino-acid sequences of the alpha and beta chains of adult hemoglobins of the Grand Galago, Galago crassicaudatus.

The adult Grand Galago (Galago crassicaudatus) was found to have two hemoglobin components (Hb I and Hb II) which were separated by carboxymethyl cellulose column chromatography. The alpha and beta chains of each component were isolated. The tryptic peptides of the alpha and beta chains were each isolated and sequenced by the conventional method. The alignment of these peptides in each chain was deduced from the homology of their sequences with that of human adult hemoglobin. The alpha chains from Hb I and Hb II were considered to be identical. On the other hand, there was only one amino-acid difference between the two beta chains at the 125th residue from the N-terminus.

Amino Acid Sequence↗
PubMed1985

Amino-acid sequences of the two major components of adult hemoglobins from the stump-tail monkey, Macaca speciosa.

The adult Stump-Tail Monkey (Macaca speciosa) was found to have two major hemoglobin components (Hb 1 and Hb 2) which were separated by carboxymethyl cellulose column chromatography. The tryptic peptides of the alpha and beta chains from the two components were isolated and sequenced. The peptides were aligned based on the homology of their sequences with that of human adult hemoglobin. Only one amino-acid difference was found between the alpha chains from Hb 1 and Hb 2 at the 15th position from the N-terminus. On the other hand, the beta chains from the two hemoglobin components were considered to be identical.

Amino Acid Sequence↗
PubMed1984

Amino acid sequences of the regulatory light chains of striated adductor muscle myosins from Ezo giant scallop and Akazara scallop.

Amino acid sequences of the regulatory light chains of striated adductor muscle myosin from Ezo giant scallop (Patinopecten yessoensis) and akazara scallop (Chlamys nipponensis akazara) were determined. Tryptic peptides of each light chain were isolated and sequenced. The alignment of the tryptic peptides in each chain was deduced from the amino acid compositions and the partial sequences of peptic peptides of the Ezo giant scallop light chain. The light chains both consist of 156 residues. Heterogeneous residues, glutamic acid and aspartic acid were observed at the 155th position in the sequence of the akazara scallop light chain. A comparison of the Ezo giant scallop light chain with the glutamic acid-containing and aspartic acid-containing akazara light chains revealed 6 and 7 amino acid substitutions, respectively. When the presented sequences were compared with those of the regulatory light chains of gizzard, cardiac and skeletal muscle myosins, a strong homology was observed in the calcium binding region, but there were considerable heterogeneities in the N- and C-terminal regions.

Amino Acid Sequence↗
PubMed1984

Complete amino acid sequence of Scytalidium lignicolum acid protease B.

The acid protease B (SLB) of Scytalidium lignicolum was reduced and carboxymethylated and then subjected to tryptic digestion. Five fragments were isolated and some of them were further digested with alpha-chymotrypsin, thermolysin, and dilute acetic acid. The sequence analysis of these fragments and the peptides by conventional methods established the complete amino acid sequence of SLB. The enzyme was composed of 204 amino acid residues with threonine and valine as its amino- and carboxyl-termini, respectively. Locations of three disulfide bridges were also established to be Cys47-126, Cys140-163, and Cys192-201 by enzymatic fragmentation of the denatured and unmodified SLB. Only a slight homology was found in the sequences of SLB and other acid proteases hitherto reported.

Amino Acid Sequence↗
PubMed1984

Primary structures of adult hemoglobins of silvery marmoset, Callithrix argentatus, and cotton-headed tamarin, Saguinus oedipus.

Tryptic peptides of the alpha and beta chains from silvery marmoset (Callithrix argentatus) and cotton-headed tamarin (Saguinus oedipus) hemoglobins were isolated and sequenced, respectively, by conventional methods. The ordering of the peptides in each chain was deduced from the homology of their sequences with those of human adult hemoglobin. The primary structures thus deduced are compared with those of other primate hemoglobins, and the rate of evolution in New World monkey hemoglobins is discussed.

Amino Acid Sequence↗
PubMed1984

Antibody against 25,000 dalton tryptic fragment of subfragment-1 from chicken skeletal muscle myosin: functional implication of the 25,000 fragment region in subfragment-1.

Antibody was prepared against the 25,000-dalton tryptic fragment of subfragment-1 from skeletal muscle myosin. The antibody was found to inhibit the Mg2+-ATPase activity and the initial P1-burst of the ATPase. The antibody suppressed the ATP-induced fluorescence enhancement of S-1, though it did not suppress the binding of ATP to S-1. The acto-S-1 ATPase activity was also inhibited by the antibody. These results suggest that there is a site in the 25K fragment region responsible for the transition of the myosin-ATP complex to another high energy complex.

Adenosine Triphosphatases↗
PubMed1984

The early adaptive evolution of calmodulin.

Interaction between gene duplication and natural selection in molecular evolution was investigated utilizing a phylogenetic tree constructed by the parsimony procedure from amino acid sequences of 50 calmodulin-family protein members. The 50 sequences, belonging to seven protein lineages related by gene duplication (calmodulin itself, troponin-C, alkali and regulatory light chains of myosin, parvalbumin, intestinal calcium-binding protein, and glial S-100 phenylalanine-rich protein), came from a wide range of eukaryotic taxa and yielded a denser tree (more branch points within each lineage) than in earlier studies. Evidence obtained from the reconstructed pattern of base substitutions and deletions in these ancestral loci suggests that, during the early history of the family, selection acted as a transforming force on expressed genes among the duplicates to encode molecular sites with new or modified functions. In later stages of descent, however, selection was a conserving force that preserved the structures of many coadapted functional sites. Each branch of the family was found to have a unique average tempo of evolutionary change, apparently regulated through functional constraints. Proteins whose functions dictate multiple interaction with several other macromolecules evolved more slowly than those which display fewer protein-protein and protein-ion interactions, e.g., calmodulin and next troponin-C evolved at the slowest average rates, whereas parvalbumin evolved at the fastest. The history of all lineages, however, appears to be characterized by rapid rates of evolutionary change in earlier periods, followed by slower rates in more recent periods. A particularly sharp contrast between such fast and slow rates is found in the evolution of calmodulin, whose rate of change in earlier eukaryotes was manyfold faster than the average rate over the past 1 billion years. In fact, the amino acid replacements in the nascent calmodulin lineage occurred at residue positions that in extant metazoans are largely invariable, lending further support to the Darwinian hypothesis that natural selection is both a creative and a conserving force in molecular evolution.

Amino Acid Sequence↗
PubMed1983

The light chains of muscle myosin: its structure, function, and evolution.

In this review I described the primary structures of myosin light chains contained in fast skeletal muscle, cardiac muscle, and gizzard muscle of chicken. In a comparison of these proteins many more amino acid substitutions than expected were recognized among the primary structures in the muscle from various organs. A fairly high homology was however shown between their primary structure, and this homology is also recognized among the light chains, parvalbumins, troponins C, and calmodulins. On the other hand, the relation between the primary structures and physiological function of these myosin light chains or the interaction between light chains and heavy chains still seems unclear. These problems are important subjects for future study.

Amino Acid Sequence↗
PubMed1982

Differences in chemical structure around the reactive lysine residues in the burst and the nonburst heads of skeletal muscle myosin.

Our laboratory has presented strong evidence for the nonidentical two-headed structure of skeletal muscle myosin. We previously showed that each of the two kinds of heads, i.e., the burst head, which forms the myosin-P-ADP complex, and the nonburst head, which forms the myosin-ATP complex upon reaction with ATP, contains 1 mol of reactive lysine residue per mol which is modified rapidly with TNBS. We also found that in the presence of PPi only the reactive lysine residue in the burst head is modified with TNBS. Utilizing this phenomenon, we presented evidence [(1981) J. Biochem. 89, 831-839] indicating that the chemical structures around the reactive lysine residues in the burst and the nonburst head are different. In this study, we determined the amino acid sequence around the reactive lysine residues to demonstrate the nonidentical chemical structure of the two heads of skeletal muscle myosin. We found that the sequence around the reactive lysine residue in the burst head was ....Pro-Met-Asn-Pro-Pro-Lys-Tyr.... and the sequence in the nonburst head was ....Ser-Met-Asn-Pro-Pro-Lys-Tyr..... Thus, a proline residue located ner the reactive lysine residue in the burst head was found to be replaced by a serine residue in the nonburst head.

Adenosine Diphosphate↗
PubMed1982

Amino-acid sequence of the L-1 light chain of chicken fast skeletal-muscle myosin.

The L-1 light chain of myosin, extracted from chicken fast skeletal-muscle, was digested with trypsin after S-carboxymethylation. The tryptic peptides in the digest were separated and purified and the amino-acid compositions and sequences of the tryptic peptides analysed. The carboxymethylated L-1 light chain was also digested with pepsin and the peptic peptides in the digest were separated and purified. The amino-acid compositions and the partial sequences of peptic peptides were analysed. From these results, the primary structure of the L-1 light chain of chicken fast skeletal-muscle myosin was determined. The established sequence consists of 190 amino acids.

Amino Acid Sequence↗
PubMed1981

Amino-acid sequence of the L-4 light chain of chicken skeletal-muscle myosin.

Tryptic and peptic peptides of the L-4 light chain of chicken skeletal muscle myosin were isolated. The amino acid sequences of all the tryptic peptides were determined. The alignment of the tryptic peptides in the protein was deduced from their homology with the primary structure of the A2 (L-4) light chain of rabbit skeletal muscle myosin. The compositions of the peptic peptides confirmed the alignment. Comparing the whole sequence of the L-4 light chain thus established with that of the A2 light chain of rabbit skeletal muscle myosin, 24 amino acid substitutions were recognized.

Amino Acid Sequence↗
PubMed1981

Amino-acid sequence of the 20 000-molecular-weight light chain of chicken gizzard-muscle myosin.

The light chain fraction was separated from chicken gizzard muscle myosin. After S-carboxymethylation or performic acid oxidation, two light chain components (20 000-Mr and 17 000-Mr chains) were isolated by chromatography on a column of DEAF-cellulose in the presence of 4 M urea. Tryptic peptides of the S-carboxymethylated 20 000-Mr chain were isolated, and their sequences were determined. The alignment of these tryptic peptides in the chain was deduced from the amino acid compositions and from the partial sequences of peptic peptide of the oxidized protein. The established sequence consists of 171 amino acids and its calculated molecular weight is 19692. Comparing the sequence with those of L-2 chains from chicken and rabbit skeletal muscle myosins, 81 and 78 amino acid substitutions were recognized, respectively, including insertions and/or deletions.

Amino Acid Sequence↗
PubMed1981

The primary structure of adult hemoglobin of musk shrew (Suncus murinus).

An alpha chain and two beta chains beta I and beta II) were obtained from adult hemoglobin of the musk shrew (Suncus murinus) by CM-cellulose column chromatography. The S-carboxymethylated alpha chain and the S-aminoethylated beta chains were each digested with trypsin and the amino acid sequences of the tryptic peptides obtained were established. The ordering of these peptides in the alpha and beta chains was deduced from their homology with the primary structures of the alpha and beta chains of human adult hemoglobin. The sequence of the alpha chain thus determined indicated to be heterogeneous at the 15th position from the N-terminus. On the other hand, comparing the primary structure of beta I chain with that of beta II chain, 4 amino acid exchanges were recognized. Further, the primary structures of the alpha and beta chains of musk shrew hemoglobin were compared with those of alpha and beta chains of human and European hedgehog hemoglobins.

Amino Acid Sequence↗
PubMed1980

Amino-acid sequence of the L-1 light chain of chicken cardiac-muscle myosin.

The light chain fraction was separated from myosin extracted from chicken cardiac muscle. Two light chain components, L-1 and L-2 in the fraction were isolated by chromatography on a column of DEAE-cellulose (DE-52) in the presence of4 M urea. After performic acid oxidation, the L-1 chain was digested with trypsin and the resulting peptides were isolated. The amino acid sequences of the peptides were established. The ordering of these tryptic peptides in the L-1 chain was deduced from the amino acid compositions and the partial sequences of peptic peptides from S-carboxymethylated L-1 chain. Comparing the whole sequence of the L-1 chain thus established with that of alkali light chain of rabbit skeletal muscle myosin, 67 amino acid substitutions and two insertions were recognized.

Amino Acid Sequence↗
PubMed1980

The primary structure of L-asparaginase from Escherichia coli.

The carboxymethylated L-asparaginase from Escherichia coli A-1--3 was fragmented with cyanogen bromide and the resulting peptides were isolated by using gel filtration on Sephadex G-50 and column chromatography on DE-52. The amino acid sequences of the 7 cyanogen bromide peptides thus obtained were established completely or partially by further fragmentation with trypsin, chymotrypsin and pepsin, and the Dansyl Edman method. Based on the above results and the complete sequences of the tryptic peptides from the carboxymethylated L-asparaginase reported in the previous paper, the whole sequence of the enzyme was established. The reported sequence consists of 321 amino acid residues and its calculated molecular weight is 34 080.

Amino Acid Sequence↗
PubMed1980

The amino acid sequence of the L-2 light chain of chicken skeletal muscle myosin.

The L-2 light chain of chicken skeletal muscle myosin was isolated and carboxymethylated. The L-2 light chain was digested with trypsin. The tryptic peptides thus obtained were separated and purified. The amino acid compositions and sequences of the tryptic peptides were analyzed. The primary structure of the L-2 light chain of chicken skeletal muscle myosin was determined by comparing the amino acid sequences of these tryptic peptides with the amino acid sequence of the L-2 light chain from rabbit skeletal muscle myosin.

Amino Acid Sequence↗