Purification and characterization of a novel isoform of mast cell tryptase from rat tongue.

Purification and characterization of a novel isoform of mast cell tryptase from rat tongue. Research Abstract Details 

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Purification and characterization of a novel isoform of mast cell tryptase from rat tongue. Abstract Text:

Y Okumura,A Kudoh,M Takashima,M Inoue,K Sakai,H Kido,

Rat mast cell tryptase was purified to homogeneity from rat tongue by a series of standard chromatographic procedures. Since the enzyme gave band corresponding to molecular mass of 32-35 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis and exhibited a molecular mass of 135 kDa on gel filtration, it was presumed to be a noncovalently associated tetramer. The N-terminal amino acid sequence of 50 residues of the enzyme showed the highest degree of homology with the same region in mouse mast cell protease 7 (92%), and less homology to those of tryptases from man and dog, and peritoneal cells of rats and Mongolian gerbils. The inhibitor specificity of rat tongue tryptase was similar to that of rat peritoneal mast cell tryptase free from trypstatin: it was inhibited by alpha 1-antitrypsin, Kunitz-type soybean trypsin inhibitor and Bowman-Birk soybean trypsin inhibitor, but these inhibitors do not inhibit the tryptases from rat skin, human lung, and dog mast cells. Judging from these results, together with other enzymatic properties, the enzyme may be a novel isoform of tryptase in rat tongue. Analysis by differential staining with peroxidase-labeled lectins of the enzyme suggested that it has tri- and/or tetraantennary complex-type oligosaccharides containing a relatively high amount of sialic acid. The immunohistochemical distribution of this enzyme indicated that the reactive antigen was specific in connective tissue but not in mucosal mast cells.

Purification and characterization of a novel isoform of mast cell tryptase from rat tongue. Publishing Authors By Initials

Y Okumura,A Kudoh,M Takashima,M Inoue,K Sakai,H Kido,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: tryptases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: tryptases research

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Purification and characterization of a novel isoform of mast cell tryptase from rat tongue. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 120

Page Numbers: 856-64

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1996

Purification and characterization of a novel isoform of mast cell tryptase from rat tongue. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Purification and characterization of a novel isoform of mast cell tryptase from rat tongue. Keywords Mesh Terms:

KEYWORDS: Tryptases

MESH TERMS: enzymology

Chemical & Substance for Abstract: Purification and characterization of a novel isoform of mast cell tryptase from rat tongue. Information

Substance Name: Peptide-N4-(N-acetyl-beta-glucosaminyl)

Registry Number: EC 3.5.1.52

Grant and Affiliation Information for Purification and characterization of a novel isoform of mast cell tryptase from rat tongue.

AFFILIATION: Division of Enzyme Chemistry, School of Medicine, University of Tokushima.

Country: JAPAN

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MEDLINETA: J Biochem

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