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For studying the role of Ser132in the putative catalytic site of human lipoprotein lipase (LPL), mutant LPL cDNAs expressing LPLs with amino acid substitutions of Gly or Asn for Ser132were 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‐Gly132, or LPL‐Asn132. LPL‐Gly132hydrolyzed Triton X‐100‐triolein and tributyrin as effectively as wild‐type LPL, whereas LPL‐Asn132showed no activity. LPL‐Asn132bound to very low density lipoproteins as effectively as wild‐type LPL.

For studying the role of Ser 132in the putative catalytic site of human lipoprotein lipase (LPL), mutant LPL cDNAs expressing LPLs with amino acid substitutions of Gly or Asn for Ser 132were 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 132hydrolyzed Triton X-100-triolein and tributyrin as effectively as wild-type LPL, whereas LPL-Asn 132showed no activity. LPL-Asn 132bound to very low density lipoproteins as effectively as wild-type LPL.