Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid

Robert G. Forage; Jennifer M. Ring; Richard W. Brown; Bernard V. McInerney; Gary S. Cobon; Richard P. Gregson; David M. Robertson; Francis J. Morgan; Milton T. W. Hearn; Jock K. Findlay; Richard E. H. Wettenhall; Henry G. Burger; David M. de Kretser

doi:10.1073/pnas.83.10.3091

Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid

Robert G. Forage, Jennifer M. Ring, Richard W. Brown, Bernard V. McInerney, Gary S. Cobon, Richard P. Gregson, David M. Robertson, Francis J. Morgan, Milton T. W. Hearn, Jock K. Findlay, Richard E. H. Wettenhall, Henry G. Burger, David M. de Kretser

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264 Citations (Scopus)

Abstract

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 (M_r = 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 (M_r = 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 OrkDa (A(C)) and 15 kDa (B), is derived from the 58-kDa form by proteolytic processing of the A subunit.

Original language	English
Pages (from-to)	3091-3095
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	83
Issue number	10
DOIs	https://doi.org/10.1073/pnas.83.10.3091
Publication status	Published - May 1986
Externally published	Yes

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Forage, R. G., Ring, J. M., Brown, R. W., McInerney, B. V., Cobon, G. S., Gregson, R. P., Robertson, D. M., Morgan, F. J., Hearn, M. T. W., Findlay, J. K., Wettenhall, R. E. H., Burger, H. G., & de Kretser, D. M. (1986). Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid. Proceedings of the National Academy of Sciences of the United States of America, 83(10), 3091-3095. https://doi.org/10.1073/pnas.83.10.3091

@article{c050993d1c5d4a0aadee34b62d29d6fc,

title = "Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid",

abstract = "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 OrkDa (A(C)) and 15 kDa (B), is derived from the 58-kDa form by proteolytic processing of the A subunit.",

author = "Forage, {Robert G.} and Ring, {Jennifer M.} and Brown, {Richard W.} and McInerney, {Bernard V.} and Cobon, {Gary S.} and Gregson, {Richard P.} and Robertson, {David M.} and Morgan, {Francis J.} and Hearn, {Milton T. W.} and Findlay, {Jock K.} and Wettenhall, {Richard E. H.} and Burger, {Henry G.} and {de Kretser}, {David M.}",

year = "1986",

month = may,

doi = "10.1073/pnas.83.10.3091",

language = "English",

volume = "83",

pages = "3091--3095",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

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Forage, RG, Ring, JM, Brown, RW, McInerney, BV, Cobon, GS, Gregson, RP, Robertson, DM, Morgan, FJ, Hearn, MTW, Findlay, JK, Wettenhall, REH, Burger, HG & de Kretser, DM 1986, 'Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid', Proceedings of the National Academy of Sciences of the United States of America, vol. 83, no. 10, pp. 3091-3095. https://doi.org/10.1073/pnas.83.10.3091

Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid. / Forage, Robert G.; Ring, Jennifer M.; Brown, Richard W. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, No. 10, 05.1986, p. 3091-3095.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid

AU - Forage, Robert G.

AU - Ring, Jennifer M.

AU - Brown, Richard W.

AU - McInerney, Bernard V.

AU - Cobon, Gary S.

AU - Gregson, Richard P.

AU - Robertson, David M.

AU - Morgan, Francis J.

AU - Hearn, Milton T. W.

AU - Findlay, Jock K.

AU - Wettenhall, Richard E. H.

AU - Burger, Henry G.

AU - de Kretser, David M.

PY - 1986/5

Y1 - 1986/5

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AB - 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 OrkDa (A(C)) and 15 kDa (B), is derived from the 58-kDa form by proteolytic processing of the A subunit.

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Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid

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