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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.
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
August 1996,
Biochimica et biophysica acta,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
November 1996,
Structure (London, England : 1993),
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
January 2006,
Biochimica et biophysica acta,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
January 2005,
Biochimica et biophysica acta,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
January 1991,
Methods in enzymology,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
November 2000,
Biochimie,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
August 1997,
Archives of biochemistry and biophysics,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
January 2004,
The Journal of nutrition,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
November 1998,
The Journal of biological chemistry,
F Carrière, and
K Thirstrup, and
S Hjorth, and
E Boel
January 1978,
Biochimie,
