Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs.

Research output: Contribution to journalArticle

121 Citations (Scopus)

Abstract

We have cloned and identified mRNA sequences for two rat pancreatic trypsinogens. Nucleotide sequence analysis of the cloned sequences revealed two mRNAs that encode similar, though noallelic, pretrypsinogens. Trypsinogen I mRNA is 804 nucleotides in length, plus an estimated poly(A) tract of 100 nucleotides, and contains a short (13 nucleotide) 5' noncoding region and a 3' noncoding region of 54 nucleotides. It encodes a preproenzyme of 246 amino acids comprising a hydrophobic prepeptide (signal peptide) of 15 amino acids, an activation peptide characteristic of trypsinogens, and an active form of trypsin, 223 amino acids in length, that has 78% amino acid sequence identity with porcine trypsin. Trypsinogen II mRNA has a nucleotide sequence 88% homologous with that of trypsinogen I mRNA and encodes a protein with 89% amino acid sequence identity with trypsinogen I. The enzymes encoded by trypsinogen I and II mRNAs retain the key amino acid residues that determine the characteristic substrate cleavage preference of trypsins and, therefore, represent the rat counterparts of this digestive enzyme. Trypsinogen I mRNA is a major pancreatic mRNA comprising an estimated 2-5% of the total, whereas trypsinogen II mRNA is present at much lower levels.

Original languageEnglish (US)
Pages (from-to)9724-9732
Number of pages9
JournalJournal of Biological Chemistry
Volume257
Issue number16
StatePublished - Aug 25 1982

Fingerprint

Trypsinogen
Rats
Nucleotides
Complementary DNA
Messenger RNA
Amino Acids
Trypsin
trypsinogen activation peptide
Amino Acid Sequence
Aminoacylation
Poly A
Enzymes
Protein Sorting Signals
Sequence Analysis
Swine

ASJC Scopus subject areas

  • Biochemistry

Cite this

Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs. / MacDonald, R. J.; Stary, S. J.; Swift, G. H.

In: Journal of Biological Chemistry, Vol. 257, No. 16, 25.08.1982, p. 9724-9732.

Research output: Contribution to journalArticle

@article{061eb8fe49ed47a3bbaa4b925b6bb01e,
title = "Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs.",
abstract = "We have cloned and identified mRNA sequences for two rat pancreatic trypsinogens. Nucleotide sequence analysis of the cloned sequences revealed two mRNAs that encode similar, though noallelic, pretrypsinogens. Trypsinogen I mRNA is 804 nucleotides in length, plus an estimated poly(A) tract of 100 nucleotides, and contains a short (13 nucleotide) 5' noncoding region and a 3' noncoding region of 54 nucleotides. It encodes a preproenzyme of 246 amino acids comprising a hydrophobic prepeptide (signal peptide) of 15 amino acids, an activation peptide characteristic of trypsinogens, and an active form of trypsin, 223 amino acids in length, that has 78{\%} amino acid sequence identity with porcine trypsin. Trypsinogen II mRNA has a nucleotide sequence 88{\%} homologous with that of trypsinogen I mRNA and encodes a protein with 89{\%} amino acid sequence identity with trypsinogen I. The enzymes encoded by trypsinogen I and II mRNAs retain the key amino acid residues that determine the characteristic substrate cleavage preference of trypsins and, therefore, represent the rat counterparts of this digestive enzyme. Trypsinogen I mRNA is a major pancreatic mRNA comprising an estimated 2-5{\%} of the total, whereas trypsinogen II mRNA is present at much lower levels.",
author = "MacDonald, {R. J.} and Stary, {S. J.} and Swift, {G. H.}",
year = "1982",
month = "8",
day = "25",
language = "English (US)",
volume = "257",
pages = "9724--9732",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "16",

}

TY - JOUR

T1 - Two similar but nonallelic rat pancreatic trypsinogens. Nucleotide sequences of the cloned cDNAs.

AU - MacDonald, R. J.

AU - Stary, S. J.

AU - Swift, G. H.

PY - 1982/8/25

Y1 - 1982/8/25

N2 - We have cloned and identified mRNA sequences for two rat pancreatic trypsinogens. Nucleotide sequence analysis of the cloned sequences revealed two mRNAs that encode similar, though noallelic, pretrypsinogens. Trypsinogen I mRNA is 804 nucleotides in length, plus an estimated poly(A) tract of 100 nucleotides, and contains a short (13 nucleotide) 5' noncoding region and a 3' noncoding region of 54 nucleotides. It encodes a preproenzyme of 246 amino acids comprising a hydrophobic prepeptide (signal peptide) of 15 amino acids, an activation peptide characteristic of trypsinogens, and an active form of trypsin, 223 amino acids in length, that has 78% amino acid sequence identity with porcine trypsin. Trypsinogen II mRNA has a nucleotide sequence 88% homologous with that of trypsinogen I mRNA and encodes a protein with 89% amino acid sequence identity with trypsinogen I. The enzymes encoded by trypsinogen I and II mRNAs retain the key amino acid residues that determine the characteristic substrate cleavage preference of trypsins and, therefore, represent the rat counterparts of this digestive enzyme. Trypsinogen I mRNA is a major pancreatic mRNA comprising an estimated 2-5% of the total, whereas trypsinogen II mRNA is present at much lower levels.

AB - We have cloned and identified mRNA sequences for two rat pancreatic trypsinogens. Nucleotide sequence analysis of the cloned sequences revealed two mRNAs that encode similar, though noallelic, pretrypsinogens. Trypsinogen I mRNA is 804 nucleotides in length, plus an estimated poly(A) tract of 100 nucleotides, and contains a short (13 nucleotide) 5' noncoding region and a 3' noncoding region of 54 nucleotides. It encodes a preproenzyme of 246 amino acids comprising a hydrophobic prepeptide (signal peptide) of 15 amino acids, an activation peptide characteristic of trypsinogens, and an active form of trypsin, 223 amino acids in length, that has 78% amino acid sequence identity with porcine trypsin. Trypsinogen II mRNA has a nucleotide sequence 88% homologous with that of trypsinogen I mRNA and encodes a protein with 89% amino acid sequence identity with trypsinogen I. The enzymes encoded by trypsinogen I and II mRNAs retain the key amino acid residues that determine the characteristic substrate cleavage preference of trypsins and, therefore, represent the rat counterparts of this digestive enzyme. Trypsinogen I mRNA is a major pancreatic mRNA comprising an estimated 2-5% of the total, whereas trypsinogen II mRNA is present at much lower levels.

UR - http://www.scopus.com/inward/record.url?scp=0020491017&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020491017&partnerID=8YFLogxK

M3 - Article

VL - 257

SP - 9724

EP - 9732

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 16

ER -