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Open AccessJournal ArticleDOI

Evolutionary constancy of primary structure in an α(A)-chain fragment of fibrinogen

T. Söderqvist, +1 more
- 01 May 1970 - 
- Vol. 7, Iss: 4, pp 321-323
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TLDR
Evidence for further sequence isologies in the or(A)-chain of different species gives evidence for the narrow substrate specificity of thrombin when acting on fibrinogen during blood clotting.
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This article is published in FEBS Letters.The article was published on 1970-05-01 and is currently open access. It has received 8 citations till now.

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Journal ArticleDOI

The molecular structure of fibrinogen.

TL;DR: This work has shown that aggregating proteins are also common in invertebrates in which cellular mechanisms primarily are responsible for hemostasis, and that the alignment of the fibrinogen units seems to determine the substrate specificity of factor XI11 in the cross-linking reaction.
Journal ArticleDOI

Primary structure of human fibrinogen and fibrin. I. Clevage of fibrinogen with cyanogen bromide. Isolation and characterization of NH 2 -terminal fragments of the ("A") chain.

TL;DR: Evidence is presented for the occurrence in the α(A) and α(AP) chain preparations of the chain variants α(AY) andα(AYP) and the relation between structure and function of fibrinogen is discussed.
Journal ArticleDOI

Primary structure of human fibrinogen and fibrin. II. Structural studies on NH2-terminal part of gamma chain.

TL;DR: The γ chain fragment observed upon electrophoresis in polyacrylamide gels is probably due to microheterogeneity of its carbohydrate moiety, and some differences in specificity of trypsin, plasmin, and thrombin when acting on theγ chain are discussed.
Journal ArticleDOI

The mechanism of the fibrinogen-thrombin reaction

TL;DR: It is proposed that the binding which is of fundamental importance takes place within the sequence 1–23 of this chain and may even be localised to the sequence 8–16.
References
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Journal ArticleDOI

Dithiothreitol, a New Protective Reagent for SH Groups*

W. Wallace Cleland
- 01 Apr 1964 - 
TL;DR: Strominger, J. L. H. (1960), Instruction Manual and Handbook, Beckman/Spinco Model 120 Amino Acid Analyzer, Palo Alto, California,Beckman Instruments Inc., Spinco Division.
Journal ArticleDOI

A specific and sensitive assay for disulfides.

TL;DR: A specific and sensitive assay for disulfide groups has been developed, based on reduction with dithioerythritol or dithiothreitol and determination of the resulting monothiols with 5,5'-dithiobis(2-nitrobenzoic acid) in the presence of arsenite.
Journal ArticleDOI

Fibrinogen Detroit--a molecular defect in the N-terminal disulphide knot of human fibrinogen?

TL;DR: Fibrinogen from a patient with a blood coagulation disorder has an amino-acid substitution (arginine to serine) in the vicinity of the bond split by thrombin during normal blood coagenation.
Journal ArticleDOI

N-Terminal Disulphide Knot of Human Fibrinogen

TL;DR: The three peptide chains in fibinogen are cross-linked at the N-terminal end of the molecule in a firm disulphide knot.
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