Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity.

Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. Abstract Text:

S Odani,T Ikenaka,

Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. Publishing Authors By Initials

S Odani,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:

Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 74

Page Numbers: 857-60

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1973

Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. Keywords Mesh Terms:

KEYWORDS: Trypsin Inhibitors

MESH TERMS: analysis

Chemical & Substance for Abstract: Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. Information

Substance Name: Chymotrypsin

Registry Number: EC 3.4.21.1

Grant and Affiliation Information for Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity 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.