Bovine angiotensin-converting enzyme: Amino-terminal sequence analysis and preliminary characterization of a hybridization-selected primary translation product

Daret K.St Clair; Kathleen A. Presper; Peter L. Smith; David C. Stump; Edward C. Heath

doi:10.1016/S0006-291X(86)80138-3

Bovine angiotensin-converting enzyme: Amino-terminal sequence analysis and preliminary characterization of a hybridization-selected primary translation product

Daret K.St Clair, Kathleen A. Presper, Peter L. Smith, David C. Stump, Edward C. Heath

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

8 Scopus citations

Abstract

Bovine lung angiotensin-converting enzyme was isolated in pure form and the sequence of the first twenty-two NH₂-terminal amino acids determined. Oligonucleotides, complementary to a selected portion of the NH₂-terminal amino acid sequence of the bovine glycoprotein (M_r 145,000), were synthesized and used for hybridization selection of angiotensin-converting enzyme mRNA. The hybridization-selected mRNA programmed the in vitro synthesis of a single polypeptide (M_r 130,000) that was specifically immunoadsorbed by anti- bovine enzyme antibodies. Preliminary sequence analysis of the primary translation product suggests that bovine angiotensin-converting enzyme is synthesized without a transient NH₂-terminal signal sequence.

Original language	English
Pages (from-to)	968-972
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	141
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(86)80138-3
State	Published - Dec 30 1986

Bibliographical note

Funding Information:
This investigation was supported by National Institutes of Health Grant AM 19850. DCS is recipient of an NHLBI Clinical Investigator Award HL01176. The authors dedicate this paper to Dr. Edward C. Heath who created the critical scientific environment for this study but whose untimely death preceded the preparation of this manuscript.

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(86)80138-3

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title = "Bovine angiotensin-converting enzyme: Amino-terminal sequence analysis and preliminary characterization of a hybridization-selected primary translation product",

abstract = "Bovine lung angiotensin-converting enzyme was isolated in pure form and the sequence of the first twenty-two NH2-terminal amino acids determined. Oligonucleotides, complementary to a selected portion of the NH2-terminal amino acid sequence of the bovine glycoprotein (Mr 145,000), were synthesized and used for hybridization selection of angiotensin-converting enzyme mRNA. The hybridization-selected mRNA programmed the in vitro synthesis of a single polypeptide (Mr 130,000) that was specifically immunoadsorbed by anti- bovine enzyme antibodies. Preliminary sequence analysis of the primary translation product suggests that bovine angiotensin-converting enzyme is synthesized without a transient NH2-terminal signal sequence.",

author = "Clair, {Daret K.St} and Presper, {Kathleen A.} and Smith, {Peter L.} and Stump, {David C.} and Heath, {Edward C.}",

note = "Funding Information: This investigation was supported by National Institutes of Health Grant AM 19850. DCS is recipient of an NHLBI Clinical Investigator Award HL01176. The authors dedicate this paper to Dr. Edward C. Heath who created the critical scientific environment for this study but whose untimely death preceded the preparation of this manuscript.",

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doi = "10.1016/S0006-291X(86)80138-3",

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Bovine angiotensin-converting enzyme: Amino-terminal sequence analysis and preliminary characterization of a hybridization-selected primary translation product. / Clair, Daret K.St; Presper, Kathleen A.; Smith, Peter L. et al.
In: Biochemical and Biophysical Research Communications, Vol. 141, No. 3, 30.12.1986, p. 968-972.

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

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T1 - Bovine angiotensin-converting enzyme

T2 - Amino-terminal sequence analysis and preliminary characterization of a hybridization-selected primary translation product

AU - Clair, Daret K.St

AU - Presper, Kathleen A.

AU - Smith, Peter L.

AU - Stump, David C.

AU - Heath, Edward C.

N1 - Funding Information: This investigation was supported by National Institutes of Health Grant AM 19850. DCS is recipient of an NHLBI Clinical Investigator Award HL01176. The authors dedicate this paper to Dr. Edward C. Heath who created the critical scientific environment for this study but whose untimely death preceded the preparation of this manuscript.

PY - 1986/12/30

Y1 - 1986/12/30

N2 - Bovine lung angiotensin-converting enzyme was isolated in pure form and the sequence of the first twenty-two NH2-terminal amino acids determined. Oligonucleotides, complementary to a selected portion of the NH2-terminal amino acid sequence of the bovine glycoprotein (Mr 145,000), were synthesized and used for hybridization selection of angiotensin-converting enzyme mRNA. The hybridization-selected mRNA programmed the in vitro synthesis of a single polypeptide (Mr 130,000) that was specifically immunoadsorbed by anti- bovine enzyme antibodies. Preliminary sequence analysis of the primary translation product suggests that bovine angiotensin-converting enzyme is synthesized without a transient NH2-terminal signal sequence.

AB - Bovine lung angiotensin-converting enzyme was isolated in pure form and the sequence of the first twenty-two NH2-terminal amino acids determined. Oligonucleotides, complementary to a selected portion of the NH2-terminal amino acid sequence of the bovine glycoprotein (Mr 145,000), were synthesized and used for hybridization selection of angiotensin-converting enzyme mRNA. The hybridization-selected mRNA programmed the in vitro synthesis of a single polypeptide (Mr 130,000) that was specifically immunoadsorbed by anti- bovine enzyme antibodies. Preliminary sequence analysis of the primary translation product suggests that bovine angiotensin-converting enzyme is synthesized without a transient NH2-terminal signal sequence.

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Bovine angiotensin-converting enzyme: Amino-terminal sequence analysis and preliminary characterization of a hybridization-selected primary translation product

Abstract

Bibliographical note

ASJC Scopus subject areas

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