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Biomedical subjects

G Matsuda

Publications and source records attributed to G Matsuda.

At least 73 records · Page 4Linked to original sources
PubMed1980

[Hemoglobins, XXXIII. Note on the Sequence of the hemoglobins of the horse (author's transl)].

The sequence analysis of the slow migrating component of the hemoglobins of horse was repeated with the automatic methode in the sequenator and the sequence of the beta-chains completed. In the alpha-chains the positions of alpha63 and alpha65 (Gly, Ala) and alpha82 and alpha85 (amides) were changed and the remaining 40 sequences of the beta-chains are reported. According to these data and biological contributions of other authors, the biological aspects of the primary structure and the polymorphism of the hemoglobins of the horse are discussed.

Amino Acid Sequence↗
PubMed1979

Amino acid sequences of the alpha and beta chains of adult hemoglobin of the European hedgehog, Erinaceus europaeus.

Globin prepared from hemoglobin of the European hedgehog (Erinaceus europaeus) was separated into alpha and beta polypeptide chains by chromatography on a CM 52 column. The S-aminoethylated alpha and beta chains were each digested with trypsin and the resulting peptides were isolated. The sequences of all the tryptic peptides were established. The ordering of these peptides in the alpha and beta chains was deduced from their homology with the primary structures of alpha and beta chains of human adult hemoglobin. Comparing the primary structures of the alpha and beta chains of adult hemoglobin of the European hedgehog thus obtained with those of adult hemoglobin of the tupai (Tupaia glis), 35 amino acids substitutions in the alpha chains and 30 in the beta chains were recognized.

Amino Acid Sequence↗
PubMed1979

Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli.

S-Carboxymethylated L-asparaginase was digested with trypsin and the resulting peptides were isolated by using gel filtration, ion exchange column chromatography and paper chromatography. Among the peptides thus isolated, 27 peptides were considered not to overlap and the sum of the amino acids from these 27 peptides is in good agreement with amino acid composition of the enzyme. The amino acid sequences of the peptides were determined by fragmentation with various enzymes and subtractive Edman degradation.

Amino Acid Sequence↗
PubMed1979

Amino acid sequences of the alpha and beta chains of adult hemoglobin of the brown lemur, Lemur fulvus fulvus.

Globin prepared from hemoglobin of the brown lemur (Lemur fulvus fulvus) was separated into alpha and beta chains by chromatography on a CM 52 column. The S-aminoethylated alpha and beta chains were each digested with trypsin and resulting peptides were isolated. The amino acid sequences of the tryptic peptides were established. The ordering of these peptides in the alpha and beta chains was deduced from the homology of their amino acid sequences with that of human adult hemoglobin. The primary structure of brown lemur hemoglobin thus obtained differs from that of human hemoglobin in 15 amino acids in the alpha chain and 26 in the beta chain.

Amino Acid Sequence↗
PubMed1978

Amino acid sequences of the alpha and beta chains of adult hemoglobin of the slender loris, Loris tardigradus.

alpha and beta chains from adult hemoglobin of the slender loris (Loris tardigradus) were isolated by Amberlite CG-50 column chromatography. After S-aminoethylation, both chains were digested with trypsin and the amino acid sequences of the tryptic peptides obtained were analyzed. Further, the order of these tryptic peptides in each chain was deduced from their homology with the primary structures of alpha and beta chains of human adult hemoglobin. Comparing the primary structures of the alpha and beta chains of adult hemoglobin of the slender loris thus obtained with those of adult hemoglobin of the slow loris, 4 amino acid substitutions in the alpha chains and 2 in the beta chains were recognized.

Amino Acid Sequence↗
PubMed1978

The amino acid compositions of the tryptic, chymotryptic and peptic peptides from the L-2 light chain of rabbit skeletal muscle myosin.

The light chain fraction was separated from rabbit skeletal muscle myosin and four kinds of light chains, L-1, L-2, L-3 and L-4 in the fraction were further isolated by column chromatography using DEAE-cellulose DE-52. After amino-ethylation, the L-2 light chain was digested with trypsin. It was also digested with chymotrypsin and pepsin, respectively, after carboxymethylation. Each of the tryptic, chymotryptic and peptic peptides thus obtained was separated and purified and their amino acid compositions were analyzed.

Amino Acids↗
PubMed1978

The amino acid sequences of the tryptic, chymotryptic and peptic peptides from the L-2 light chain of rabbit skeletal muscle myosin.

The amino acid sequences of the tryptic peptides from the aminoethylated L-2 light chain of rabbit skeletal muscle myosin were determined by various enzymatic hydrolyses, partial hydrolysis with dilute acetic acid and Edman degradation. The amino acid sequences of the chymotryptic and peptic peptides from the carboxymethylated L-2 light chain were partially analysed in the same manner as the tryptic peptides. The primary structure of the L-2 light chain of rabbit skeletal muscle myosin was deduced from the above results.

Amino Acid Sequence↗
PubMed1977

Amino acid sequence of the L-2 light chain of rabbit skeletal muscle myosin.

The L-2 light chain (DTNB light chain) was separated from rabbit skeletal muscle myosin and the amino acid sequence determined. In order to study the primary structure of the L-2 lihe amino acid seqence determined. Then, to determine the arrangement of these tryptic peptides, enzymatic partial hydrolysis using 0.25 M acetic acid were carried out. The primary structure of the L-2 light chain thus obtained contains 168 amino acids.

Amino Acid Sequence↗
PubMed1977

Amino acid sequences of the aplpha and beta chains of adult hemoglobin of the tupai, Tupaia glis.

Globin prepared from hemoglobin of adult tupai (Tupaia glis) was separated into alpha and beta polypeptide chains by CM-cellulose column chromatography. The S-aminoethylated alpha polypeptide chain and S-carboxymethylated beta polypeptide chain were each digested with trypsin, and the sequences of all the peptides thus obtained were established. The ordering of these tryptic peptides in the alpha and beta polypeptide chains was deduced from the homology of their primary structures with that of human adult hemoglobin. In this way the primary structures of the alpha and beta polypeptide chains of tupai hemoglobin were established; 27 amino acids in the alpha polypeptide chain and 26 in the beta chain differ from those in human adult hemoglobin.

Amino Acid Sequence↗
PubMed1975

Tryptic peptides from the beta polypeptide chain of AII component of chicken hemoglobin.

The aminoethylated beta polypeptide chain in AII component from the hemoglobin of adult chicken was digested with trypsin [EC 3.4.21.4] and the resulting peptides were separated and purified by ion exchange chromatography, paper chromatography, and gel filtration. Eighteen tryptic peptides, which were nonoverlapping, accounted for all of the amino acid residues in the beta polypeptide chain. The amino acid sequences of the tryptic peptides were established by a combination of enzymatic digestion and subtractive Edman degradation.

Amino Acid Sequence↗
PubMed1975

Peptic peptides from the beta polypeptide chain of AII component of chicken hemoglobin.

The aminoethylated beta polypeptide chain of AII component from chicken hemoglobin was digested with pepsin [EC 3.4.23.1] and the resulting peptides were separated and purified by gel filtration, ion exchange chromatography, and paper chromatography. The amino acid composition and partial sequence of the peptic peptides were studied. From the results thus obtained, the primary structure of the beta polypeptide chain was established, taking account of the amino acid sequences of the tryptic peptides previously reported.

Amino Acid Sequence↗
PubMed1975

Amino acid sequence of the alpha chain of chicken AI hemoglobin.

Adult chicken hemoglobin is heterogeneous and contains two major components, AI and AII (1). The amino acid sequence of the alpha chain of the AI component from white leghorns (small A type) was determined and compared with that of the alpha chain of the AII component, previously determined by the authors (2). An unexpectedly large difference of 65 amino acids was found between these two chains.

Amino Acid Sequence↗