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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/4508


    Title: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase
    Authors: Martin GA;Busch SJ;Meredith GD;Cardin AD;Blankenship DT;Mao SJT;Rechtin AE;Woods CW;Racke MM;Schafer MP;Fitzgerald MC;Burke DM;Flanagan MA;Jackson RL
    Contributors: Department of Biotechnology
    Date: 1988-08
    Issue Date: 2009-11-26 09:43:29 (UTC+8)
    Publisher: Asia University
    Abstract: Hepatic triglyceride lipase (H-TGL) was isolated from human postheparin plasma by column chromatography on heparin-Sepharose and phenyl-Sepharose and immunoaffinity chromatography with monoclonal antibodies. The purified enzyme had an apparent molecular weight of 65,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and an amino-terminal sequence of Leu-Gly-Gln-Ser-Leu-Lys-Pro-Glu. Partial amino acid sequences of seven cyanogen bromide peptides were obtained. A human hepatoma cDNA library was screened with synthetic oligonucleotides derived from the partial protein sequence. The cloned H-TGL cDNA of 1569 nucleotides predicts a mature protein of 477 amino acids plus a leader sequence of 22 amino acids. Blot hybridization analysis of poly(A)+ mRNA with a putative H-TGL cDNA clone gave a single hybridizing band of 1.7 kilobases. The protein contains four consensus N-glycosylation sequences based on the cDNA sequence. Comparison of the enzyme sequence with that of other lipases reveals highly conserved sequences in regions of putative lipid and heparin binding. The carboxyl terminus of H-TGL contains a highly basic sequence which is not reported to be present in rat H-TGL or other members of the lipase gene family.
    Relation: The Journal of Biological Chemistry 263(22):10907-14
    Appears in Collections:[Department of Biotechnology] Journal Article

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