Recombinant bile salt activated lipases

Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing – Hydrolases

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435198, 536 232, 536 2431, A61K 3754, C12N 1555, C12N 920

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active

052001830

ABSTRACT:
The complete structure of human milk BAL cDNA is disclosed. The nucleotide sequences of the cDNA inserts of two clones overlap and together contain 2951 base pairs of BAL cDNA which codes for an open reading frame of 742 amino acid residues between initiation and termination codons. There is a putative signal sequence of 20 residues which is followed by a 61-amino-terminal sequence of BAL. The cDNA sequence also contains a 678-base 5'-untranslated sequence, a 97-base 3'-untranslated region, and a 14-base poly(A) tail. The deduced BAL protein structure contains in the carboxyl-terminal region fourteen repeating unis of 11 amino acids each. The repeating units have the basic structure of Pro-Val-Pro-Pro-Thr-Gly-Asp-Ser-Gly-Ala-Pro-, with only minor substitutions. The cDNA is useful for expression of protein, study of structure, function and the effect of modification or deletion or addition of amino acids, including entire repeating units, and as probes for studies involving BAL or related lipases, including rat pancreatic lysophospholipase, cholinesterase, and acetylcholinesterase.

REFERENCES:
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Kyger et al., Biochem. Biophys. Res. Comm., vol. 164, No. 3 (Nov. 15, 1989), pp. 1302-1309.
Han et al., Biochemistry, vol. 26, 1617-1625 (1987).
Wang, Biochem. Biophys. Res. Comm., vol. 155, No. 2 (1988) pp. 950-955.
Young et al., PNAS USA, vol. 80 (Mar. 1983), 1194-1198.
Martin et al., Journal of Biological Chemistry, vol. 263, No. 22, 1988, pp. 10907-10914.
Chi-Sun Wang, et al., Analytical Biochemistry 133:457-461 (1983).

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