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 activator
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference35 articles.
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1. Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone‐like activities of bovine seminal plasma protein PDC‐109;FEBS Letters;2019-10-09
2. Spermine and spermidine act as chemical chaperones and enhance chaperone-like and membranolytic activities of major bovine seminal plasma protein, PDC-109;Biochemical and Biophysical Research Communications;2017-12
3. Evolution and function of mammalian binder of sperm proteins;Cell and Tissue Research;2015-09-19
4. Biophysical Characterization of the Interaction of O-acylcholines with the Major Bovine Seminal Plasma Protein, PDC-109;Advances in Experimental Medicine and Biology;2014-11-03
5. Top-down mass spectrometry reveals new sequence variants of the major bovine seminal plasma protein PDC-109;Journal of Mass Spectrometry;2012-07
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