Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product.

Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product. Abstract Text:

Y Hishikawa-Itoh,I Sugie,H Kato,S Iwanaga,

A factor, named SK-potentiator, which is known to potentiate the activation of plasminogen by streptokinase (SK), was isolated from human plasma. The procedures consisted of column chromatographies on DEAE-Sephadex A-50 and heparin-agarose, followed with gel-filtration on a Sepharose 6B column and affinity chromatography on a lysine-Sepharose 4B column. The isolated SK-potentiator markedly potentiated the rate of activation of plasminogen by streptokinase. However, it did not show a potentiating effect on the activation of plasminogen by urokinase or on the plasmin activity. SK-potentiator showed a similar mobility to that of fibrinogen on both SDS-polyacrylamide gel and agarose gel electrophoresis, and cross-reacted with anti-fibrinogen antiserum. The amino acid composition of SK-potentiator was very close to that of human fibrinogen, although the content of serine and threonine was significantly lower. SK-potentiator showed a single band with a molecular weight of 300,000 on SDS-gel electrophoresis in the absence of 2-mercaptoethanol. In the presence of 2-mercaptoethanol, it showed two major bands with molecular weights of 53,000 and 48,000, respectively, which corresponded to the B beta chain and gamma chain of fibrinogen. To establish further that the isolated SK-potentiator may be one of the fibrinogen degradation products (FDP), human fibrinogen was digested with plasmin and the SK-potentiator activity generated in the course of the digestion was measured. As a result, the SK-potentiator activity was found to initially increase and then decrease with incubation time, suggesting that an early FDP has the ability to potentiate the SK-mediated activation of plasminogen. The early FDP was then isolated by gel-filtration on a column of Sepharose 6B and it was found that the SK-potentiator activity was associated with the early FDP. Moreover, the early FDP showed the same electrophoretic mobility as the isolated SK-potentiator on SDS-gel electrophoresis and their amino acid compositions were quite similar to each other. From these results, the SK-potentiator was identified as the early FDP.

Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product. Publishing Authors By Initials

Y Hishikawa-Itoh,I Sugie,H Kato,S Iwanaga,

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

PUBMED ID PMID:

MEDLINE DATE:

Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 92

Page Numbers: 1129-40

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1982

Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product. Keywords Mesh Terms:

KEYWORDS: Streptokinase

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product. Information

Substance Name: Plasminogen Activators

Registry Number: EC 3.4.21.-

Grant and Affiliation Information for Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Streptokinase-dependent potentiating factor SK-potentiator for plasminogen activation from human plasma: its identification as a fibrinogen degradation product Related Publications

• A method for preparation of a single chain high-molecular-weight (HMW) kininogen from bovine plasma.
• A method for systematic purification from bovine plasma of six vitamin K-dependent coagulation factors: prothrombin, factor X, factor IX, protein S, protein C, and protein Z.
• A new method for purification of staphylocoagulase by a bovine prothrombin-Sepharose column.
• Accelerating effect of zinc ions on the surface-mediated activation of factor XII and prekallikrein.
• Activation of factor XII and prekallikrein with polysaccharide sulfates and sulfatides: comparison with kaolin-mediated activation.
• Amino acid sequence of Japanese horseshoe crab (Tachypleus tridentatus) coagulogen B chain: completion of the coagulogen sequence.
• Characterization of serine proteinases isolated from rat submaxillary gland: with special reference to the degradation of rat kininogens by these enzymes.
• Fibrinogens Kawaguchi and Osaka: an amino acid substitution of A alpha arginine-16 to cysteine which forms an extra interchain disulfide bridge between the two A alpha chains.
• Identification of the plasminogen-binding site of human alpha 2-plasmin inhibitor.
• Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes.
• Interaction of factor XII, high-molecular-weight (HMW) kininogen and prekallikrein with sulfatide: analysis by fluorescence polarization.
• Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties.
• Isolation and amino acid sequence of a peptide containing an epoxide-reactive residue from the thermolysin-digest of Scytalidium lignicolum acid protease B.
• Isolation and characterization of the polypeptide chain involved in the cross-linking of stabilized bovine fibrin.
• Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein.
• Mechanism of surface-mediated activation of bovine factor XII and plasma prekallikrein.
• Nucleotide sequence of the staphylocoagulase gene: its unique COOH-terminal 8 tandem repeats.
• Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus.
• Primary structure of bovine plasma low-molecular-weight kininogen. The complete amino acid sequence of COOH-terminal portion following the bradykinin moiety.
• Proteolytic cleavage of vitamin K-dependent bovine plasma protein S by alpha-thrombin and plasma serine protease.
• Purification and amino acid sequence of Kunitz-type protease inhibitor found in the hemocytes of horseshoe crab (Tachypleus tridentatus).
• Purification and properties of intracellular clotting factor, factor B, from horseshoe crab (Tachypleus tridentatus) hemocytes.
• Purification and properties of prothrombin activator from the venom of Echis carinatus.
• Streptokinase-dependent potentiating factor (SK-potentiator) for plasminogen activation from human plasma: its identification as a fibrinogen degradation product.
• Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC mapping.
• The amino acid sequence of coagulogen isolated from southeast Asian horseshoe crab, Tachypleus gigas.
• The complete amino acid sequence of coagulogen isolated from Southeast Asian horseshoe crab, Carcinoscorpius rotundicauda.
• The role of bovine high-molecular-weight (HMW) kininogen in contact-mediated activation of bovine factor XII: interaction of HMW kininogen with kaolin and plasma prekallikrein.
• Two types of coagulogen mRNAs found in horseshoe crab (Tachypleus tridentatus) hemocytes: molecular cloning and nucleotide sequences.
• [Non-bacterial thrombotic endocarditis]