Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid.
Open Access
- 1 May 1992
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (14) , 10149-10155
- https://doi.org/10.1016/s0021-9258(19)50212-5
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Platelet Activating Factor Activity in the Phospholipids of Bovine Spermatozoa1Biology of Reproduction, 1990
- Annexins—New family of Ca2+-regulated-phospholipid binding proteinBioscience Reports, 1987
- Common domain structure of Ca2+ and lipid‐binding proteinsFEBS Letters, 1986
- The PDC-109 protein from bovine seminal plasma is similar to the gelatin-binding domain of bovine fibronectin and a kringle domain of human tissue-type plasminogen activatorBiochemical and Biophysical Research Communications, 1985
- Structure of human factor VIIINature, 1984
- Primary structure of PDC-109, a major protein constituent of bovine seminal plasmaBiochemical and Biophysical Research Communications, 1983
- Surface Proteins and Glycoproteins of Ejaculated Bovine Spermatozoa. I. Iodination and Proteolytic DigestionBiology of Reproduction, 1981
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970