Structural identity of immunoglobulin binding factor and prostatic secretory protein of human seminal plasma.
The amino acid sequence of the N-terminus of the immunoglobulin binding factor of human seminal plasma was determined. The initial 30 amino acids showed complete identity with that of prostatic secretory protein, beta-microseminoprotein and beta-inhibin. In conclusion, these proteins are probably a single entity.
Center for Biomedical Research, Population Council, New York, NY 10021.
Z G
ZG
Liang
M
M
Kamada
S S
SS
Koide
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D006801:Humans; D007265:Inhibins / Q000737:chemistry; D008222:Lymphokines / Q000737:chemistry*; D008297:Male; D008969:Molecular Sequence Data; D011467:Prostate / Q000737:chemistry; D029584:Prostatic Secretory Proteins; D011506:Proteins / Q000737:chemistry*; D012661:Semen / Q000737:chemistry*; D029589:Seminal Plasma Proteins; D012689:Sequence Homology, Nucleic Acid
D002352:Carrier Proteins; D008222:Lymphokines; D029584:Prostatic Secretory Proteins; D011506:Proteins; D029589:Seminal Plasma Proteins; C043076:beta-microseminoprotein; C028321:estramustine-binding protein; C013059:immunoglobulin-binding factors; D007265:Inhibins