Rat preprocarboxypeptidase A

cDNA sequence and preliminary characterization of the gene

C. Quinto, M. Quiroga, W. F. Swain, W. C. Nikovits, D. N. Standring, R. L. Pictet, P. Valenzuela, W. J. Rutter

Resultado de la investigación: Article

67 Citas (Scopus)

Resumen

Rat carboxypeptidase A cDNA clones have been isolated from a cDNA library prepared from pancreatic mRNA. An almost complete mRNA sequence has been deduced that predicts a polypeptide having 75% amino acid sequence homology with bovine carboxypeptidase A. The amino acid sequence of the activation and signal peptides of the carboxypeptidase A precursor were inferred from the nucleotide sequence. The cDNA was used as a probe to identify DNA fragments containing carboxypeptidase A sequences in a bacteriophage λ library of rat genomic DNA. Heteroduplexes revealed that the DNA coding sequence occupies 5.5 kilobases and is interrupted by nine intervening sequences. The nucleotide sequence of the 5' end of the gene and the adjacent flanking region provides information on the site of initiation of transcription and the putative control regions. There is no evident relationship between the localization of intervening sequences in the gene and functional/structural domains of the protein.

Idioma originalEnglish
Páginas (desde-hasta)31-35
Número de páginas5
PublicaciónProceedings of the National Academy of Sciences of the United States of America
Volumen79
N.º1
EstadoPublished - 1982

Huella dactilar

Carboxypeptidases A
Complementary DNA
Introns
Genes
Nucleic Acid Heteroduplexes
Amino Acid Sequence Homology
Messenger RNA
Genomic Library
Transcription Initiation Site
DNA
Protein Sorting Signals
Gene Library
Bacteriophages
Amino Acid Sequence
Clone Cells
Peptides
preprocarboxypeptidase A

ASJC Scopus subject areas

  • Genetics
  • General

Citar esto

Quinto, C., Quiroga, M., Swain, W. F., Nikovits, W. C., Standring, D. N., Pictet, R. L., ... Rutter, W. J. (1982). Rat preprocarboxypeptidase A: cDNA sequence and preliminary characterization of the gene. Proceedings of the National Academy of Sciences of the United States of America, 79(1), 31-35.
Quinto, C. ; Quiroga, M. ; Swain, W. F. ; Nikovits, W. C. ; Standring, D. N. ; Pictet, R. L. ; Valenzuela, P. ; Rutter, W. J. / Rat preprocarboxypeptidase A : cDNA sequence and preliminary characterization of the gene. En: Proceedings of the National Academy of Sciences of the United States of America. 1982 ; Vol. 79, N.º 1. pp. 31-35.
@article{8b5f9b6bad2043849fea8e7120118ef3,
title = "Rat preprocarboxypeptidase A: cDNA sequence and preliminary characterization of the gene",
abstract = "Rat carboxypeptidase A cDNA clones have been isolated from a cDNA library prepared from pancreatic mRNA. An almost complete mRNA sequence has been deduced that predicts a polypeptide having 75{\%} amino acid sequence homology with bovine carboxypeptidase A. The amino acid sequence of the activation and signal peptides of the carboxypeptidase A precursor were inferred from the nucleotide sequence. The cDNA was used as a probe to identify DNA fragments containing carboxypeptidase A sequences in a bacteriophage λ library of rat genomic DNA. Heteroduplexes revealed that the DNA coding sequence occupies 5.5 kilobases and is interrupted by nine intervening sequences. The nucleotide sequence of the 5' end of the gene and the adjacent flanking region provides information on the site of initiation of transcription and the putative control regions. There is no evident relationship between the localization of intervening sequences in the gene and functional/structural domains of the protein.",
author = "C. Quinto and M. Quiroga and Swain, {W. F.} and Nikovits, {W. C.} and Standring, {D. N.} and Pictet, {R. L.} and P. Valenzuela and Rutter, {W. J.}",
year = "1982",
language = "English",
volume = "79",
pages = "31--35",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "1",

}

Quinto, C, Quiroga, M, Swain, WF, Nikovits, WC, Standring, DN, Pictet, RL, Valenzuela, P & Rutter, WJ 1982, 'Rat preprocarboxypeptidase A: cDNA sequence and preliminary characterization of the gene', Proceedings of the National Academy of Sciences of the United States of America, vol. 79, n.º 1, pp. 31-35.

Rat preprocarboxypeptidase A : cDNA sequence and preliminary characterization of the gene. / Quinto, C.; Quiroga, M.; Swain, W. F.; Nikovits, W. C.; Standring, D. N.; Pictet, R. L.; Valenzuela, P.; Rutter, W. J.

En: Proceedings of the National Academy of Sciences of the United States of America, Vol. 79, N.º 1, 1982, p. 31-35.

Resultado de la investigación: Article

TY - JOUR

T1 - Rat preprocarboxypeptidase A

T2 - cDNA sequence and preliminary characterization of the gene

AU - Quinto, C.

AU - Quiroga, M.

AU - Swain, W. F.

AU - Nikovits, W. C.

AU - Standring, D. N.

AU - Pictet, R. L.

AU - Valenzuela, P.

AU - Rutter, W. J.

PY - 1982

Y1 - 1982

N2 - Rat carboxypeptidase A cDNA clones have been isolated from a cDNA library prepared from pancreatic mRNA. An almost complete mRNA sequence has been deduced that predicts a polypeptide having 75% amino acid sequence homology with bovine carboxypeptidase A. The amino acid sequence of the activation and signal peptides of the carboxypeptidase A precursor were inferred from the nucleotide sequence. The cDNA was used as a probe to identify DNA fragments containing carboxypeptidase A sequences in a bacteriophage λ library of rat genomic DNA. Heteroduplexes revealed that the DNA coding sequence occupies 5.5 kilobases and is interrupted by nine intervening sequences. The nucleotide sequence of the 5' end of the gene and the adjacent flanking region provides information on the site of initiation of transcription and the putative control regions. There is no evident relationship between the localization of intervening sequences in the gene and functional/structural domains of the protein.

AB - Rat carboxypeptidase A cDNA clones have been isolated from a cDNA library prepared from pancreatic mRNA. An almost complete mRNA sequence has been deduced that predicts a polypeptide having 75% amino acid sequence homology with bovine carboxypeptidase A. The amino acid sequence of the activation and signal peptides of the carboxypeptidase A precursor were inferred from the nucleotide sequence. The cDNA was used as a probe to identify DNA fragments containing carboxypeptidase A sequences in a bacteriophage λ library of rat genomic DNA. Heteroduplexes revealed that the DNA coding sequence occupies 5.5 kilobases and is interrupted by nine intervening sequences. The nucleotide sequence of the 5' end of the gene and the adjacent flanking region provides information on the site of initiation of transcription and the putative control regions. There is no evident relationship between the localization of intervening sequences in the gene and functional/structural domains of the protein.

UR - http://www.scopus.com/inward/record.url?scp=0020059494&partnerID=8YFLogxK

M3 - Article

VL - 79

SP - 31

EP - 35

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 1

ER -