Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein.

Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein. Research Abstract Details 

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Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein. Abstract Text:

K Kodama,H Kato,S Iwanaga,

A possible role of bovine platelets in the surface-mediated activation of Factor XII and prekallikrein was studied, using the contact system reconstituted with the purified proteins from bovine plasma. The washed platelets before and after aggregation by ADP, thrombin or collagen did not show any ability to trigger or accelerate the activation of Factor XII and prekallikrein. On the contrary, these aggregates showed a potent inhibitory activity on the activation of those zymogens triggered by kaolin, amylose sulfate and sulfatide. The inhibitory substances from the supernatant of the thrombin-induced aggregates were separated into two major fractions, a low affinity fraction and a high affinity fraction, on a heparin-Sepharose column. The high affinity protein was identified as platelet factor 4, based on the amino acid composition. From the low affinity fraction, a beta-thromboglobulin (beta-TG)-like substance and three kinds of unknown proteins, named LA1, LA2, and LA3, were isolated by gel-filtration on a column of Sephadex G-100 or Sephadex G-75 followed by chromatography on a column of Mono S. The molecular weights of LA1, LA2, and LA3 were estimated to be 35,000, 26,000, and 11,000, respectively, on SDS-PAGE. LA2 was identified as a carbohydrate-less LA1, as judged from the amino acid composition and carbohydrate content. The inhibitory activities of these five cationic proteins on the activation of Factor XII and prekallikrein mediated with amylose sulfate, sulfatide and kaolin were different from each other. In the case of kaolin-mediated activation, LA3 was the most potent inhibitor, while platelet factor 4 and beta-TG-like substance did not show any significant inhibitory activity. Moreover, the inhibitory activities of all the cationic proteins were not correlated with their anti-heparin activities. Since these proteins were rapidly liberated from platelets by the action of the stimulants, the present results demonstrate a negative role of platelets in the surface-mediated activation of Factor XII and prekallikrein.

Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein. Publishing Authors By Initials

K Kodama,H Kato,S Iwanaga,

For similar peptides: intercellular signaling peptides and proteins: cytokines: chemokines: beta-thromboglobulin research abstracts see: peptides: intercellular signaling peptides and proteins: cytokines: chemokines: beta-thromboglobulin research

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Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 97

Page Numbers: 139-51

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 1985

Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein. Keywords Mesh Terms:

KEYWORDS: beta-Thromboglobulin

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Isolation of bovine platelet cationic proteins which inhibit the surface-mediated activation of factor XII and prekallikrein. Information

Substance Name: Thrombin

Registry Number: EC 3.4.21.5

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Country: JAPAN

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MEDLINETA: J Biochem

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