Association of annexin V with prolactin in the rat anterior pituitary gland.
When pituitary extracts were subjected to non denaturing polyacrylamide gel electrophoresis, an unknown protein was found to associate with a proportion of the prolactin. This protein was dissociated from prolactin by sodium dodecyl sulfate. The protein was purified and sequenced. As the amino terminus was blocked, the amino acid sequences of three peptide fragments were determined. The obtained sequences of 41 amino acids were identical to partial sequences of a known protein, rat Annexin V. The molecular mass, 36 kDa, was also the same as the molecular weight of Annexin V. The existence of Annexin V mRNA in rat pituitary glands was also confirmed by polymerase chain reaction. These results show that Annexin V, a member of the calcium-dependent phospholipid binding proteins, is synthesized in the rat pituitary gland, and suggest its association with prolatin in the gland.
Kawaminami
M
M
Laboratory of Veterinary Physiology, School of Veterinary Medicine and Animal Sciences, Kitasato University, Aomori, Japan.
Tanaka
K
K
Asawa
T
T
Osugi
S
S
Kawauchi
H
H
Kurusu
S
S
Hashimoto
I
I
D000818:Animals; D017304:Annexin A5; D002135:Calcium-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008565:Membrane Proteins / Q000302:isolation & purification; D008970:Molecular Weight; D010903:Pituitary Gland, Anterior / Q000737:chemistry*; D011257:Pregnancy Proteins / Q000302:isolation & purification* / Q000378:metabolism; D011388:Prolactin / Q000302:isolation & purification* / Q000378:metabolism; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains
D017304:Annexin A5; D002135:Calcium-Binding Proteins; D008565:Membrane Proteins; D011257:Pregnancy Proteins; D011388:Prolactin