Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties.

Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties. Abstract Text:

T Nakamura,T Morita,S Iwanaga,

A proclotting enzyme associated with the hemolymph coagulation system of limulus (Tachypleus tridentatus) was highly purified from the hemocyte lysate. The first step of purification was performed by chromatography of the lysate on a pyrogen-free dextran sulfate-Sepharose CL-6B column, which was essential for separation of the proclotting enzyme from its activator, named factor B. The following steps consisted of column chromatographies on DEAE-Sepharose CL-6B, Sephadex G-150, benzamidine-CH-Sepharose and Sephacryl S-300. Through these procedures, 1.4 mg of the purified material was obtained from 630 ml of the lysate and approximately 300-fold purification was achieved. The preparation gave a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the presence and absence of 2-mercaptoethanol. The single-chain proclotting enzyme was a glycoprotein with an apparent molecular weight of 54,000, and no gamma-carboxyglutamic acid was detected. The proclotting enzyme was converted to its active form by purified factor B or by trypsin. The resulting clotting enzyme had a molecular weight of 54,000, consisting of a heavy chain of Mr = 31,000 and a light chain of Mr = 25,000. The serine active site of the clotting enzyme was found in the heavy chain. The chemical analyses of the isolated heavy and light chains indicated that the activation of the proclotting enzyme to its active form by factor B or trypsin is induced by a limited proteolysis, yielding two chains bridged by a disulfide linkage(s).

Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties. Publishing Authors By Initials

T Nakamura,T Morita,S Iwanaga,

For similar natural sciences: chemistry: chemistry, physical: molecular weight research abstracts see: natural sciences: chemistry: chemistry, physical: molecular weight research

PUBMED ID PMID:

MEDLINE DATE:

Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 97

Page Numbers: 1561-74

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 1985

Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties. Keywords Mesh Terms:

KEYWORDS: Molecular Weight

MESH TERMS: enzymology

Chemical & Substance for Abstract: Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties. Information

Substance Name: pro-clotting enzyme

Registry Number: EC 3.4.99.-

Grant and Affiliation Information for Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Intracellular proclotting enzyme in limulus Tachypleus tridentatus hemocytes: its purification and properties 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]