Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid.
The primary amino acid structures of the 43-kDa (A) and 15-kDa (B) subunits of the 58-kDa form of the hormone inhibin have been elucidated by cloning and analysis of cDNA species derived from bovine granulosa cell mRNA. The A subunit (Mr = 32,298) is a protein of 300 amino acids with two potential N-glycosylation sites and two potential proteolytic processing sites and has a pre-pro region of 60 amino acids. The mature B subunit (Mr = 12,977) is a protein of 116 amino acids synthesized from a separate mRNA. These data establish that a 31-kDa form of inhibin also isolated from bovine follicular fluid, with subunits of 20 kDa (Ac) and 15 kDa (B), is derived from the 58-kDa form by proteolytic processing of the A subunit.
Forage
R G
RG
Ring
J M
JM
Brown
R W
RW
McInerney
B V
BV
Cobon
G S
GS
Gregson
R P
RP
Robertson
D M
DM
Morgan
F J
FJ
Hearn
M T
MT
Findlay
J K
JK
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005260:Female; D007265:Inhibins / Q000235:genetics*; D008970:Molecular Weight; D006080:Ovarian Follicle / Q000502:physiology
D007265:Inhibins; D004247:DNA