Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors.

Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. Abstract Text:

M Yamamoto,T Ikenaka,

Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. Publishing Authors By Initials

M Yamamoto,T Ikenaka,

For similar chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: protease inhibitors: serine proteinase inhibitors: trypsin inhibitors research abstracts see: chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: protease inhibitors: serine proteinase inhibitors: trypsin inhibitors research

PUBMED ID PMID:

MEDLINE DATE:

Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 62

Page Numbers: 141-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 1967

Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. Keywords Mesh Terms:

KEYWORDS: Trypsin Inhibitors

MESH TERMS: analysis

Chemical & Substance for Abstract: Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. Information

Substance Name: Trypsin Inhibitors

Registry Number: 0

Grant and Affiliation Information for Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Studies on soybean trypsin inhibitors I Purification and characterization of two soybean trypsin inhibitors Related Publications

• A study on the interaction of soybean trypsin inhibitor with trypsin by circular dichroism.
• Amino acid sequences of fragments I and II obtained by cyanogen bromide cleavage of rat serum albumin.
• Characterization of a peptide released during the reaction of human alpha 1-antitrypsin and bovine alpha-chymotrypsin.
• Circular dichroism and optical rotatory dispersion of trypsin inhibitors.
• Comparative study of carbohydrate-protein complexes. II. Determination of hydroxylysine and its glycosides in human skin and scar collagens by an improved method.
• Fragmentation of rat serum albumin by cyanogen bromide cleavage and the amino acid sequences of four fragments.
• Human alpha1-antitrypsin. Characterization and N- and C-terminal sequences.
• Importance of the carboxyl-terminal four amino acid residues in the inhibitory activity of Streptomyces subtilisin inhibitor (with a revision of its carboxyl-terminal sequence).
• Isolation and characterization of an N-linked oligosaccharide that is significantly increased in sera from patients with non-small cell lung cancer.
• Isolation and characterization of three forms of cathepsin B from porcine liver.
• Location of the essential thiol of porcine liver cathepsin B.
• Proteinase inhibitors from a mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz).
• Reinvestigation on the amino acid composition and C-terminal group of Taka-amylase A.
• Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity.
• States of tyrosyl residues and circular dichroism of Kunitz trypsin inhibitor.
• Structure of Streptomyces erythraeus lysozyme at 6 A resolution.
• Studies on soybean trypsin inhibitors, XII. Linear sequences of two soybean double-headed trypsin inhibitors, D-II and E-I.
• Studies on soybean trypsin inhibitors. 3. Isolation and sequence determination of the tryptic peptides of Bowman-Birk soybean proteinase inhibitor.
• Studies on soybean trypsin inhibitors. 8. Disulfide bridges in soybean Bowman-Birk proteinase inhibitor.
• Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors.
• Studies on soybean trypsin inhibitors. II. Accidentally modified Kunitz soybean trypsin inhibitor.
• Studies on soybean trypsin inhibitors. IV. Change of the inhibitory activity of Bowman-Birk inhibitor upon replacements of the alpha-chymotrypsin reactive site serine residue by other amino acids.
• Studies on soybean trypsin inhibitors. IV. Complete amino acid sequence and the anti-proteinase sites of Bowman-Birk soybean proteinase inhibitor.
• Studies on soybean trypsin inhibitors. X. Isolation and partial characterization of four soybean double-headed proteinase inhibitors.
• Studies on soybean trypsin inhibitors. XI. Complete amino acid sequence of a soybean trypsin-chymotrypsin-elastase inhibitor, C-II.
• Studies on soybean trypsin inhibitors. XIII. Preparation and characterization of active fragments from Bowman-Birk proteinase inhibitor.
• The amino acid sequence of soybean trypsin inhibitor (Kunitz).
• The amino acid sequences of glycopeptides obtained from Taka-amylase A with trypsin and chymotrypsin.
• The amino acid sequences of two soybean double headed proteinase inhibitors and evolutionary consideration on the legume proteinase inhibitors.
• The reactive site of Streptomyces subtilisin inhibitor.