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

Producción científica: Article › revisión exhaustiva

8 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	968-972
Número de páginas	5
Publicación	Biochemical and Biophysical Research Communications
Volumen	141
N.º	3
DOI	https://doi.org/10.1016/S0006-291X(86)80138-3
Estado	Published - dic 30 1986

Nota bibliográfica

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.

Financiación

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.

Financiadores	Número del financiador
National Institutes of Health (NIH)	AM 19850

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.",

year = "1986",

month = dec,

day = "30",

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.
En: Biochemical and Biophysical Research Communications, Vol. 141, N.º 3, 30.12.1986, p. 968-972.

Producción científica: Article › revisión exhaustiva

TY - JOUR

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

M3 - Article

C2 - 3028395

AN - SCOPUS:0022910921

SN - 0006-291X

VL - 141

SP - 968

EP - 972

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

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

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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