Light and heavy fractions of fragment D: preparation and examination of fibrin-binding properties

V. A. Belitser; T. M. Pozdnjakova; T. P. Ugarova

doi:10.1016/0049-3848(80)90008-0

Light and heavy fractions of fragment D: preparation and examination of fibrin-binding properties

V. A. Belitser, T. M. Pozdnjakova, T. P. Ugarova

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

Tryptic fragment D obtained from bovine fibrinogen has been divided into one heavy and two light fractions (D_H, D_LI and D_L2 respectively). Affinity chromatography on fibrin-agarose in media containing Ca²⁺ has proved most successful. D_LI possesses no affinity for immobilized fibrin whereas that of DL2 is very high. D_L2 interacts with fibrin about 3 times stronger than D_H as shown by measurements of inhibitory effects on fibrin monomer polymerization and capacities for solubilizing fibrin permanently. D_LI is fully inert.

Original language	English (US)
Pages (from-to)	807-814
Number of pages	8
Journal	Thrombosis Research
Volume	19
Issue number	6
DOIs	https://doi.org/10.1016/0049-3848(80)90008-0
State	Published - Jan 1 1980
Externally published	Yes

Keywords

affinity chromatography
complexes
fibrin
fragment D

ASJC Scopus subject areas

Hematology

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10.1016/0049-3848(80)90008-0

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title = "Light and heavy fractions of fragment D: preparation and examination of fibrin-binding properties",

abstract = "Tryptic fragment D obtained from bovine fibrinogen has been divided into one heavy and two light fractions (DH, DLI and DL2 respectively). Affinity chromatography on fibrin-agarose in media containing Ca2+ has proved most successful. DLI possesses no affinity for immobilized fibrin whereas that of DL2 is very high. DL2 interacts with fibrin about 3 times stronger than DH as shown by measurements of inhibitory effects on fibrin monomer polymerization and capacities for solubilizing fibrin permanently. DLI is fully inert.",

keywords = "affinity chromatography, complexes, fibrin, fragment D",

author = "Belitser, {V. A.} and Pozdnjakova, {T. M.} and Ugarova, {T. P.}",

year = "1980",

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doi = "10.1016/0049-3848(80)90008-0",

language = "English (US)",

volume = "19",

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journal = "Thrombosis Research",

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T1 - Light and heavy fractions of fragment D

T2 - preparation and examination of fibrin-binding properties

AU - Belitser, V. A.

AU - Pozdnjakova, T. M.

AU - Ugarova, T. P.

PY - 1980/1/1

Y1 - 1980/1/1

N2 - Tryptic fragment D obtained from bovine fibrinogen has been divided into one heavy and two light fractions (DH, DLI and DL2 respectively). Affinity chromatography on fibrin-agarose in media containing Ca2+ has proved most successful. DLI possesses no affinity for immobilized fibrin whereas that of DL2 is very high. DL2 interacts with fibrin about 3 times stronger than DH as shown by measurements of inhibitory effects on fibrin monomer polymerization and capacities for solubilizing fibrin permanently. DLI is fully inert.

AB - Tryptic fragment D obtained from bovine fibrinogen has been divided into one heavy and two light fractions (DH, DLI and DL2 respectively). Affinity chromatography on fibrin-agarose in media containing Ca2+ has proved most successful. DLI possesses no affinity for immobilized fibrin whereas that of DL2 is very high. DL2 interacts with fibrin about 3 times stronger than DH as shown by measurements of inhibitory effects on fibrin monomer polymerization and capacities for solubilizing fibrin permanently. DLI is fully inert.

KW - affinity chromatography

KW - complexes

KW - fibrin

KW - fragment D

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AN - SCOPUS:0019215367

SN - 0049-3848

VL - 19

SP - 807

EP - 814

JO - Thrombosis Research

JF - Thrombosis Research

IS - 6

ER -

Light and heavy fractions of fragment D: preparation and examination of fibrin-binding properties

Abstract

Keywords

ASJC Scopus subject areas

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