Affinity purification of seminalplasmin and characterization of its interaction with calmodulin.

Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Research Abstract Details 

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Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Abstract Text:

M Comte,A ,J A Cox,

Bull seminalplasmin antagonizes with high potency and selectivity the activating effect of calmodulin on target enzymes [Gietzen & Galla (1985) Biochem. J. 230, 277-280]. In the present paper we establish that seminalplasmin forms a 1:1, Ca2+-dependent and urea-resistant complex with calmodulin. The dissociation constant equals 1.6 nM. In the absence of Ca2+ a low-affinity complex is formed that is disrupted by 4 M-urea. On the basis of these properties, a fast affinity purification of seminalplasmin was developed. The high specificity of seminalplasmin as a calmodulin antagonist was demonstrated for the multipathway-regulated adenylate cyclase of bovine cerebellum. Far-u.v. c.d. properties are consistent with a random form of seminalplasmin in aqueous solution; 23% alpha-helix is induced on interaction with calmodulin. The fluorescence properties of the single tryptophan residue of seminalplasmin are markedly changed on formation of the complex. These studies allowed us to locate tentatively the peptide segment that interacts with calmodulin, and to ascertain the structural homology between seminalplasmin and other calmodulin-binding peptides. Additional material, showing the inhibition of calmodulin-mediated activation of bovine brain phosphodiesterase by melittin and seminalplasmin and also the near-u.v. spectrum of affinity-purified seminalplasmin, has been deposited as supplement SUP 50135 (4 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1986) 233, 5.

Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Publishing Authors By Initials

M Comte,A ,JA Cox,

For similar investigative techniques: chemistry, analytical: photometry: spectrophotometry research abstracts see: investigative techniques: chemistry, analytical: photometry: spectrophotometry research

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Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Journal Published:

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

Journal: The Biochemical journal

VOLUME: 240

Page Numbers: 567-73

Journal Abbreviation: Biochem. J.

ISSN: 0264-6021

DAY: 1

MONTH: Dec

YEAR: 1986

Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Information

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LANGUAGE: eng

NlmUniqueID: 2984726

Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Keywords Mesh Terms:

KEYWORDS: Spectrophotometry

MESH TERMS: metabolism

Chemical & Substance for Abstract: Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Information

Substance Name: Adenylate Cyclase

Registry Number: EC 4.6.1.1

Grant and Affiliation Information for Affinity purification of seminalplasmin and characterization of its interaction with calmodulin.

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Country: ENGLAND

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MEDLINETA: Biochem J

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