Seminalplasmin. An endogenous calmodulin antagonist
- 15 August 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 230 (1), 277-280
- https://doi.org/10.1042/bj2300277
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.This publication has 16 references indexed in Scilit:
- Comparison of the calmodulin antagonists compound 48/80 and calmidazoliumBiochemical Journal, 1983
- Inhibition of calmodulin activity by insect venom peptidesBiochemical Pharmacology, 1983
- A model for the regulation of the calmodulin-dependent enzymes erythrocyte Ca2+-transport ATPase and brain phosphodiesterase by activators and inhibitorsBiochemical Journal, 1982
- Inhibition by melittin of phospholipid-sensitive and calmodulin-sensitive Ca2+ -dependent protein kinasesBiochemical Journal, 1982
- Lack of tissue specificity of calmodulin: A rapid and high‐yield purification methodFEBS Letters, 1981
- Calcium-induced exposure of a hydrophobic surface on calmodulinBiochemistry, 1980
- Calmodulin Plays a Pivotal Role in Cellular RegulationScience, 1980
- An improved assay for nanomole amounts of inorganic phosphateAnalytical Biochemistry, 1979
- Seminalplasmin—an antimicrobial protein from bovine seminal plasma which acts in E. coli by specific inhibition of rRNA synthesisNature, 1979
- Sensitive automated methods for phosphate and (Na+ + K+)-ATPaseAnalytical Biochemistry, 1974