Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells

A. I. Smith; C. A. Wallace; R. L. Moritz; R. J. Simpson; L. B. Schmauk-White; E. A. Woodcock; J. W. Funder

doi:10.1677/joe.0.115R005

Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells

A. I. Smith, C. A. Wallace, R. L. Moritz, R. J. Simpson, L. B. Schmauk-White, E. A. Woodcock, J. W. Funder

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

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Abstract

Though minor sequence differences between-species have been reported for adrenocorticotrophin, ACTH(1-39), the steroidogenic moiety ACTH(1-24) has appeared invariant in mammals. We here report the isolation, purification and amino acid sequencing of guinea-pig (GP) ACTH in which Pro²⁴ is replaced by Ala²⁴, and the demonstration that GP-ACTH stimulates aldosterone production to maximal levels well above those seen with human ACTH(1-39) or Synacthen, ACTH(1-24) amide, the synthetic ACTH fragment widely used for diagnostic and therapeutic purposes.

Original language	English
Journal	Journal of Endocrinology
Volume	115
Issue number	2
DOIs	https://doi.org/10.1677/joe.0.115R005
Publication status	Published - 1 Jan 1987

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title = "Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells",

abstract = "Though minor sequence differences between-species have been reported for adrenocorticotrophin, ACTH(1-39), the steroidogenic moiety ACTH(1-24) has appeared invariant in mammals. We here report the isolation, purification and amino acid sequencing of guinea-pig (GP) ACTH in which Pro24 is replaced by Ala24, and the demonstration that GP-ACTH stimulates aldosterone production to maximal levels well above those seen with human ACTH(1-39) or Synacthen, ACTH(1-24) amide, the synthetic ACTH fragment widely used for diagnostic and therapeutic purposes.",

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doi = "10.1677/joe.0.115R005",

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T1 - Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells

AU - Smith, A. I.

AU - Wallace, C. A.

AU - Moritz, R. L.

AU - Simpson, R. J.

AU - Schmauk-White, L. B.

AU - Woodcock, E. A.

AU - Funder, J. W.

PY - 1987/1/1

Y1 - 1987/1/1

N2 - Though minor sequence differences between-species have been reported for adrenocorticotrophin, ACTH(1-39), the steroidogenic moiety ACTH(1-24) has appeared invariant in mammals. We here report the isolation, purification and amino acid sequencing of guinea-pig (GP) ACTH in which Pro24 is replaced by Ala24, and the demonstration that GP-ACTH stimulates aldosterone production to maximal levels well above those seen with human ACTH(1-39) or Synacthen, ACTH(1-24) amide, the synthetic ACTH fragment widely used for diagnostic and therapeutic purposes.

AB - Though minor sequence differences between-species have been reported for adrenocorticotrophin, ACTH(1-39), the steroidogenic moiety ACTH(1-24) has appeared invariant in mammals. We here report the isolation, purification and amino acid sequencing of guinea-pig (GP) ACTH in which Pro24 is replaced by Ala24, and the demonstration that GP-ACTH stimulates aldosterone production to maximal levels well above those seen with human ACTH(1-39) or Synacthen, ACTH(1-24) amide, the synthetic ACTH fragment widely used for diagnostic and therapeutic purposes.

UR - https://www.scopus.com/pages/publications/0023625816

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DO - 10.1677/joe.0.115R005

M3 - Article

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AN - SCOPUS:0023625816

SN - 0022-0795

VL - 115

JO - Journal of Endocrinology

JF - Journal of Endocrinology

IS - 2

ER -

Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells

Abstract

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