Biophysical Characterization of the Interaction of O-acylcholines with the Major Bovine Seminal Plasma Protein, PDC-109
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Publisher
Springer International Publishing
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http://link.springer.com/content/pdf/10.1007/978-3-319-11280-0_18
Reference35 articles.
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3. Anbazhagan V, Sankhala RS, Singh BP, Swamy MJ (2011) Isothermal titration calorimetric studies on the interaction of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes. PLoS One 6:e25993
4. Baker ME (1985) 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. Biochem Biophys Res Commun 130:1010–1014
5. Baxa U, Cooper A, Weintraub A, Pfeil W, Seckler R (2001) Enthalpic barriers to the hydrophobic binding of oligosaccharides to phage P22 tailspike protein. Biochemistry 40:5144–5150
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1. Contrasting effects of molecular crowding on the membrane-perturbing and chaperone-like activities of major bovine seminal plasma protein, PDC-109;International Journal of Biological Macromolecules;2024-01
2. Glycosylation differentially modulates membranolytic and chaperone-like activities of PDC-109, the major protein of bovine seminal plasma;Biochemical and Biophysical Research Communications;2019-03
3. Factors Influencing the Chaperone-Like Activity of Major Proteins of Mammalian Seminal Plasma, Equine HSP-1/2 and Bovine PDC-109: Effect of Membrane Binding, pH and Ionic Strength;Advances in Experimental Medicine and Biology;2018
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