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Effects of substitutions of glycine and asparagine for serine 132 on activity and binding of human lipoprotein lipase to very low density lipoproteins
Author(s) -
Tashiro Jun,
Kobayashi Junji,
Shirai Kohji,
Saito Yasushi,
Fukamachi Isamu,
Hashimoto Hideyuki,
Nishida Tsutomu,
Shibui Tatsuro,
Morimoto Yuuki,
Yoshida Sho
Publication year - 1992
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(92)80017-b
Subject(s) - glycine , serine , asparagine , biochemistry , lipase , lipoprotein lipase , chemistry , lipoprotein , enzyme , amino acid , cholesterol
For studying the role of Ser 132 in the putative catalytic site of human lipoprotein lipase (LPL), mutant LPL cDNAs expressing LPLs with amino acid substitutions of Gly or Asn for Ser 132 were obtained by site‐directed mutagenesis, and were expressed in COS‐1 cells. Considerable amounts of LPL enzyme protein mass were detected in the culture medium of COS‐1 cells transfected with wild‐type LPL, LPL‐Gly 132 , or LPL‐Asn 132 . LPL‐Gly 132 hydrolyzed Triton X‐100‐triolein and tributyrin as effectively as wild‐type LPL, whereas LPL‐Asn 132 showed no activity. LPL‐Asn 132 bound to very low density lipoproteins as effectively as wild‐type LPL.