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filingDate 1991-04-04-04:00^^<http://www.w3.org/2001/XMLSchema#date>
inventor http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_355f20528933f8721d384549206a9520
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_459a22649805e7e50acbaef3ab3777e4
publicationDate 1999-05-12-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber EP-0861897-A3
titleOfInvention Recombinant bile salt activated lipases
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 720 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 96-base 3'-untranslated region, and a 14-base poly(A) tail. The deduced BAL protein structure contains in the carboxyl-terminal region fourteen repeating units 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. <IMAGE> <IMAGE>
priorityDate 1990-04-04-04:00^^<http://www.w3.org/2001/XMLSchema#date>
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