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The cDNA sequence encoding bovine pregastric esterase

M Y Timmermans1, H Teuchy, L P Kupers

  • 1Department of Biochemistry, Limburgs Universitair Centrum, Diepenbeek, Belgium.

Gene
|September 30, 1994
PubMed
Summary
This summary is machine-generated.

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Researchers cloned the calf pregastric esterase (PGE) gene using polymerase chain reaction (PCR). The cloned PGE enzyme shares high genetic identity with human gastric lipase and rat lingual lipase.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Pregastric esterase (PGE) is a lipase found in the stomach of young ruminants.
  • Understanding the genetic and molecular characteristics of PGE is crucial for digestive physiology research.

Purpose of the Study:

  • To clone and characterize the gene encoding calf pregastric esterase (PGE).
  • To compare the genetic sequences of PGE with related lipases like human gastric lipase (HGL) and rat lingual lipase (RLL).

Main Methods:

  • Polymerase chain reaction (PCR) was employed to amplify specific gene segments.
  • A calf tongue cDNA library was screened using primers derived from conserved regions of HGL and RLL.
  • The full coding sequence of the PGE gene was subsequently cloned.

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Main Results:

  • The complete coding sequence for calf PGE was successfully cloned.
  • PGE is expressed as a mature 378-amino-acid polypeptide with a molecular mass of 42,960 Da.
  • The PGE, HGL, and RLL genes exhibit significant nucleotide and amino-acid sequence identity.

Conclusions:

  • Calf PGE shares considerable genetic homology with HGL and RLL, suggesting a common evolutionary origin.
  • PGE's active site contains a conserved Gly-Xaa-Ser-Xaa-Gly motif, characteristic of serine hydrolases.
  • PGE differs significantly from non-preduodenal lipases, highlighting its specialized role.