Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences

Raymond J. MacDonald, Galvin H. Swift, Carmen Quinto, William Swain, Raymond L. Pictet, William Nikovits, William J. Rutter

Research output: Contribution to journalArticle

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Abstract

The mRNA sequences for two rat pancreatic elastolytic enzymes have been cloned by recombinant DNA technology and their nucleotide sequences determined. Rat elastase I mRNA is 1113 nucleotides in length, plus a poly(A) tail, and encodes a preproelastase of 266 amino acids. The amino acid sequence of the predicted active form of rat elastase I is 84% homologous to porcine elastase 1. Key amino acid residues involved in determining substrate specificity of porcine elastase 1 are retained in the rat enzyme. The activation peptide of the zymogen does not appear related to that of other mammalian pancreatic serine proteases. The mRNA for elastase I is localized in the rough endoplasmic reticulum of acinar cells, as expected for the site of synthesis of an exocrine secretory enzyme. Rat elastase II mRNA is 910 nucleotides in length, plus a poly(A) tail, and encodes a preproenzyme of 271 amino acids. The amino acid sequence is more closely related to porcine elastase 1 (58% sequence identity) than to the other pancreatic serine proteases (33-39% sequence identity). Predictions of substrate preference based upon key amino acid residues that define the substrate binding cleft are consistent with the broad specificity observed for mammalian pancreatic elastase 2. The activation peptide is similar to that of the chymotrypsinogens and retains an N-terminal cysteine available to form a disulfide link to an internal conserved cysteine residue.

Original languageEnglish (US)
Pages (from-to)1453-1463
Number of pages11
JournalBiochemistry
Volume21
Issue number6
StatePublished - 1982

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Pancreatic Elastase
Sequence Analysis
Rats
RNA
Amino Acids
Messenger RNA
Swine
Nucleotides
Serine Proteases
Cysteine
Amino Acid Sequence
Substrates
Enzymes
Chemical activation
Chymotrypsinogen
Genetic engineering
Peptides
Enzyme Precursors
Recombinant DNA
Rough Endoplasmic Reticulum

ASJC Scopus subject areas

  • Biochemistry

Cite this

Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences. / MacDonald, Raymond J.; Swift, Galvin H.; Quinto, Carmen; Swain, William; Pictet, Raymond L.; Nikovits, William; Rutter, William J.

In: Biochemistry, Vol. 21, No. 6, 1982, p. 1453-1463.

Research output: Contribution to journalArticle

MacDonald, Raymond J. ; Swift, Galvin H. ; Quinto, Carmen ; Swain, William ; Pictet, Raymond L. ; Nikovits, William ; Rutter, William J. / Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned messenger ribonucleic acid sequences. In: Biochemistry. 1982 ; Vol. 21, No. 6. pp. 1453-1463.
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