High-affinity binding of seminal plasma PSP94 to human immunoglobulin is through the Fab domain
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry
Reference28 articles.
1. Characterization of a polypeptide from human seminal plasma with inhibin (inhibition of FSH secretion) like activity;Sheth;FEBS Lett.,1984
2. The amino acid sequence of human β-microseminoprotein;Akiyama;Biochim. Biophy. Acta Prot. Struc. Mol. Enz.,1985
3. Human seminal plasma beta-microseminoprotein: its purification, characterization, and immunohistochemical localization;Ohkubo;Int. J. Biochem. Cell Biol.,1995
4. Amino acid sequence of beta-microseminoprotein from porcine seminal plasma;Fernlund;Arch. Biochem. Biophys.,1994
5. Molecular cloning and gene expression analysis of PSP94 (prostate secretory protein of 94 amino acids) in primates;Xuan;DNA Cell Biol.,1997
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Structural and molecular biology of PSP94 Its significance in prostate pathophysiology;Frontiers in Bioscience;2018
2. Prostate Secretory Protein of 94 Amino Acids (PSP94) Binds to Prostatic Acid Phosphatase (PAP) in Human Seminal Plasma;PLoS ONE;2013-03-04
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