Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors.

Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors. Abstract Text:

Y Suzuki,K Yoshida,T Ichimiya,T Yamamoto,H Sinohara,

Contrapsin and two isoforms, F (fast) and S (slow), of alpha-1-antiproteinase (also called alpha-1-proteinase inhibitor) were isolated in an apparently homogeneous state from plasma of inflamed guinea pigs. Contrapsin inactivated trypsin, but did not significantly affect chymotrypsin, pancreatic elastase, or pancreatic kallikrein. On the other hand, both isoforms of alpha-1-antiproteinase inhibited trypsin, chymotrypsin, and elastase, but not plasma or pancreatic kallikrein. The S isoform of alpha-1-antiproteinase was present in barely detectable amounts in healthy animals, but increased markedly when the acute-phase reaction was induced by subcutaneous injection of turpentine. On the other hand, the plasma levels of the F isoform, contrapsin, and alpha-macroglobulin showed moderate (1.5 to 2.3-fold) elevation during the acute-phase reaction. In contrast to the previous findings that rats and rabbits contain two different alpha-macroglobulins, one of which is an acute-phase reactant while the other is not, inflamed guinea pigs contained only one species of alpha-macroglobulin. Murinoglobulin, the most prominent acute-phase negative protein in both mice and rats, showed no significant change in guinea pigs. These results indicate that guinea pig plasma contains four major trypsin inhibitors, i.e., contrapsin, alpha-1-antiproteinase, alpha-macroglobulin, and murinoglobulin, the properties of which are very similar to those of the respective mouse homologues, but that the acute-phase response of these inhibitors differs greatly from that of the homologous proteins in rats or mice.

Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors. Publishing Authors By Initials

Y Suzuki,K Yoshida,T Ichimiya,T Yamamoto,H Sinohara,

For similar peptides: proteinase inhibitory proteins, secretory: alpha 1-antitrypsin research abstracts see: peptides: proteinase inhibitory proteins, secretory: alpha 1-antitrypsin research

PUBMED ID PMID:

MEDLINE DATE:

Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 107

Page Numbers: 173-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 1990

Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors. Keywords Mesh Terms:

KEYWORDS: alpha 1-Antitrypsin

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors. Information

Substance Name: Kallikreins

Registry Number: EC 3.4.21.-

Grant and Affiliation Information for Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors.

AFFILIATION: Department of Biochemistry, Kinki University School of Medicine, Osaka.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors Related Publications

• Acute phase response of plasma proteins in analbuminemic rats.
• Amidolytic activity of porcine trypsin bound to human plasma alpha-1-antiproteinase.
• Amino acid sequence at the reactive site of rabbit alpha-1-antiproteinases.
• Changes in trypsin-binding properties and conformation of rabbit alpha-2-macroglobulin on reaction with methylamine.
• Clearance of desialylated mouse alpha-macroglobulin and murinoglobulin in the mouse.
• Cloning and sequencing of cDNA coding for rabbit alpha-1-antiproteinase F: amino acid sequence comparison of alpha-1-antiproteinases of six mammals.
• Cloning and sequencing of cDNAs encoding plasma alpha-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of alpha-macroglobulin family.
• Differential interactions of rabbit plasma alpha-1-antiproteinases S and F with porcine trypsin.
• Hamster alpha-macroglobulin and murinoglobulin: comparison of chemical and biological properties with homologs from other mammals.
• Inhibitory spectrum of mouse contrapsin and alpha-1-antitrypsin against mouse serine proteases.
• Inter-alpha-trypsin inhibitor and its related proteins in Syrian hamster urine and plasma.
• Isolation and characterization of alpha-macroglobulin from guinea pig plasma.
• Isolation and characterization of sex-steroid-binding protein from rat and rabbit plasma.
• Molecular cloning and sequence analysis of full-length cDNA coding for mouse contrapsin.
• Molecular cloning and sequencing of cDNA encoding plasma countertrypin, a member of mammalian fetuin family, from the Mongolian gerbil, Meriones unguiculatus.
• Molecular cloning and sequencing of cDNAs encoding three heavy-chain precursors of the inter-alpha-trypsin inhibitor in Syrian hamster: implications for the evolution of the inter-alpha-trypsin inhibitor heavy chain family.
• Plasma alpha-1-antiproteinase from the Mongolian gerbil, Meriones unguiculatus: isolation, partial characterization, sequencing of cDNA, and implications for molecular evolution.
• Proteinase inhibitory spectrum of mouse murinoglobulin and alpha-macroglobulin.
• Purification and characterization of rat plasma alpha-1-antitrypsin.
• Purification and characterization of testosterone-binding globulin of canine serum.
• Rabbit plasma alpha-1-antiproteinase S-1: cloning, sequencing, expression, and proteinase inhibitory properties of recombinant protein.
• Rat plasma murinoglobulin: isolation, characterization, and comparison with rat alpha-1- and alpha-2-macroglobulins.
• Subunit structure of sex-steroid-binding plasma proteins from man, cattle, dog, and rabbit.
• Trypsin inhibitors in guinea pig plasma: isolation and characterization of contrapsin and two isoforms of alpha-1-antiproteinase and acute phase response of four major trypsin inhibitors.