Literature DB >> 956151

Primary structure of bovine plasma high-molecular-weight kininogen. The amino acid sequence of a glycopeptide portion (fragment 1) following the C-terminus ot the bradykinin moiety.

Y N Han, H Kato, S Iwanaga, T Suzuki.   

Abstract

On incubation of bovine plasma high-molecular-weight (HMW) kininogen with purified plasma kallikrein [EC 3.4.21.8], a large glycopeptide fragment and the vasoactive peptide, bradykinin, were initially liberated; the former, named fragment 1-2, was subsequently cleaved into fragment 1 (glycopeptide) and the previously established fragment 2 (histidine-rich peptide). The isolated fragment 1-2 contained a total of 108 to 110 amino acid residues and carbohydrates, and the amino-terminal sequence Ser-Val-Gln was established. The other fragment, fragment 1, consisted of a total of 69 amino acid residues with serine and arginine (and lysine) at the amino and carboxyl termini, respectively. It contained eleven residues each of histidine and glycine, together with an oligosaccharide chain consisting of galactosamine, hexose and sialic acid. The complete amino acid sequence of fragment 1 was determined by Edman degradation and standard enzymatic and chemical techniques. These results established the following sequence: H-Ser-Val-Gln-Val-Met-Lys-Thr-Glu-Gly-Ser-Thr-Pro/Thr-Val-Ser(CHO)-Val/Leu-Pro-His-Ser-Ala-Met-Ser-Pro-Val-Gln-Asp-Glu-Glu-Arg-Asp-Ser-Gly-Lys-Glu-Gln-Gly-Pro-Thr-His-Gly-His-Gly-Trp-Asp-His-Gly-Lys-Gln-Ile-Lys-Leu-His-Gly-Leu-Gly-Leu-Gly-His-Lys-His-Lys-His-Asp-Gln-Gly-His-Gly-His-His-Lys/ArgOH.

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Year:  1976        PMID: 956151     DOI: 10.1093/oxfordjournals.jbchem.a131175

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  8 in total

1.  A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein.

Authors:  H Lilja
Journal:  J Clin Invest       Date:  1985-11       Impact factor: 14.808

2.  Purification of enzymes of the kallikrein gene family (rK8 and rK9) from the rat prostate.

Authors:  H Schøyen; I Wassdal; K Toft; M Almendingen; T Berg
Journal:  Biochem J       Date:  1994-08-15       Impact factor: 3.857

3.  Primary structures of bovine liver low molecular weight kininogen precursors and their two mRNAs.

Authors:  H Nawa; N Kitamura; T Hirose; M Asai; S Inayama; S Nakanishi
Journal:  Proc Natl Acad Sci U S A       Date:  1983-01       Impact factor: 11.205

4.  A putative transmembrane protein with histidine-rich charge clusters encoded in the H-2K/tw5 region of mice.

Authors:  B St-Jacques; T H Han; A MacMurray; H S Shin
Journal:  Mol Cell Biol       Date:  1990-01       Impact factor: 4.272

5.  Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells.

Authors:  R C Wiggins; D J Loskutoff; C G Cochrane; J H Griffin; T S Edgington
Journal:  J Clin Invest       Date:  1980-01       Impact factor: 14.808

6.  Early O-glycosidic glycosylation of proglucagon in pancreatic islets: an unusual type of prohormonal modification.

Authors:  C Patzelt; B Weber
Journal:  EMBO J       Date:  1986-09       Impact factor: 11.598

7.  Characterization of human high molecular weight kininogen. Procoagulant activity associated with the light chain of kinin-free high molecular weight kininogen.

Authors:  R E Thompson; R Mandle; A P Kaplan
Journal:  J Exp Med       Date:  1978-02-01       Impact factor: 14.307

8.  Relation between structure and correcting activity of bovine high molecular weight kininogen upon the clotting time of Fitzgerald-trait plasma.

Authors:  A G Scicli; R Waldmann; J A Guimaraes; G Scicli; O A Carretero; H Kato; Y N Han; S Iwanaga
Journal:  J Exp Med       Date:  1979-04-01       Impact factor: 14.307

  8 in total

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