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Literature DB >> 2996494

Seminalplasmin. An endogenous calmodulin antagonist.

Abstract

Seminalplasmin, a strongly basic protein isolated from bull semen, was found to antagonize with high potency and extraordinary specificity the function of calmodulin. Calmodulin antagonism is the result of an interaction between the two proteins, which is mainly determined by electrostatic forces. The stimulation of Ca2+-transporting ATPase and phosphodiesterase by calmodulin was half-maximally inhibited at approx. 0.1 microM-seminalplasmin. However, the basal activity of calmodulin-dependent enzymes was not significantly altered by seminalplasmin over the concentration range investigated.

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Year: 1985 PMID： 2996494 PMCID： PMC1152613 DOI： 10.1042/bj2300277

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

15 in total

8. A model for the regulation of the calmodulin-dependent enzymes erythrocyte Ca2+-transport ATPase and brain phosphodiesterase by activators and inhibitors.

Authors: K Gietzen; I Sadorf; H Bader
Journal: Biochem J Date: 1982-12-01 Impact factor: 3.857

Seminalplasmin. An endogenous calmodulin antagonist.

1. An improved assay for nanomole amounts of inorganic phosphate.

2. Sensitive automated methods for phosphate and (Na+ plus K+)-ATPase.

3. Comparison of the calmodulin antagonists compound 48/80 and calmidazolium.

4. Inhibition by melittin of phospholipid-sensitive and calmodulin-sensitive Ca2+-dependent protein kinases.

5. Lack of tissue specificity of calmodulin: a rapid and high-yield purification method.

Review 6. Calmodulin plays a pivotal role in cellular regulation.

7. Interaction of beta-endorphin and other opioid peptides with calmodulin.

8. A model for the regulation of the calmodulin-dependent enzymes erythrocyte Ca2+-transport ATPase and brain phosphodiesterase by activators and inhibitors.

9. Calcium-induced exposure of a hydrophobic surface on calmodulin.

10. Amino acid sequence of seminalplasmin, an antimicrobial protein from bull semen.

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