A
Asao Murai
Researcher at Ajinomoto
Publications - 35
Citations - 396
Asao Murai is an academic researcher from Ajinomoto. The author has contributed to research in topics: Amino acid & Mass spectrometry. The author has an hindex of 13, co-authored 35 publications receiving 385 citations.
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Journal ArticleDOI
Determination of the Tryptophan Content of Feed and Feedstuffs by Ion Exchange Liquid Chromatography
TL;DR: It was shown that co-existing nutrients, such as carbohydrate, fiber, and free or combined ash, did not affect the recovery of tryptophan in lysozyme, but that the recovery was reduced by the presence of fat and defatting of feed and feedstuffs is necessary to obtain accurate values by this method.
Journal ArticleDOI
The structure of permetin A, a new polypeptin type antibiotic produced by Bacillus circulans.
TL;DR: The structure of permetin A(I), an antibiotic substance produced by Bacillus circulans AJ 3902, has been elucidated as a cyclic acyl peptide by means of the mass and nuclear magnetic resonance spectroscopic techniques.
Journal ArticleDOI
Primary structure of Paim I, an alpha-amylase inhibitor from Streptomyces corchorushii, determined by the combination of Edman degradation and fast atom bombardment mass spectrometry.
Kazuo Hirayama,Rei Takahashi,Satoko Akashi,Ken-ichi Fukuhara,Naoki Oouchi,Asao Murai,Motoo Arai,Sawao Murao,Kazuo Tanaka,Ittetsu Nojima +9 more
TL;DR: The primary structure of Paim I has been determined by Edman degradation and fast atom bombardment mass spectrometry (FABMS), a single-chain polypeptide of 73 amino acid residues with a calculated molecular weight from the sequence data of 7415.3 (monoisotopic molecular weight).
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Conformational analysis of amino acids and peptides using specific isotope substitution. I. Conformation of L-phenylalanylglycine.
TL;DR: An attempt to explain the origin of the nonequivalence of the glycine methylene protons was made, and a conformational model for L-phenylalanylglycine is proposed.
Journal ArticleDOI
A determination of the positions of disulphide bonds in Paim I, α-amylase inhibitor from Streptomyces corchorushii, using fast atom bombardment mass spectrometry
Satoko Akashi,Kazuo Hirayama,Tadatoshi Seino,Shinichi Ozawa,Ken-ichi Fukuhara,Naoki Oouchi,Asao Murai,Motoo Arai,Sawao Murao,Kazuo Tanaka,Ittetsu Nojima +10 more
TL;DR: Paim I, a protein alpha-amylase inhibitor, is a single-chain polypeptide which consists of 73 amino acids, including 4 half-cystine residues, which has been determined with the combination of enzymatic digestion and fast atom bombardment (FAB) mass spectrometry.