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Cloning of the classical guinea pig pancreatic lipase and comparison with the lipase related protein 2
Author(s) -
Carrière Frédéric,
Thirstrup Kenneth,
Hjorth Siv,
Boel Esper
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80117-7
Subject(s) - lipase , complementary dna , pancreatic lipase , guinea pig , amino acid , microbiology and biotechnology , biochemistry , colipase , biology , cloning (programming) , enzyme , chemistry , gene , genetics , computer science , programming language
Starting from total pancreatic mRNAs, the classical guinea pig pancreatic lipase was cloned using rapid amplification of 3' and 5' cDNA ends. Internal oligonucleotide primers were designed from a partial cDNA clone including the region coding for the lid domain. Using this strategy, we did not amplify the cDNA corresponding to the pancreatic lipase related protein 2 in which the lid domain is deleted. Amino acid sequences of the classical guinea pig pancreatic lipase and the related protein 2 were compared based on the primary and tertiary structures of the classical human pancreatic lipase. Their distinct physiological roles are discussed in the light of functional amino acid differences.