Glycosylation of bile salt-dependent lipase (cholesterol esterase).

作者: Eric Mas , Marie-Odile Sadoulet , Assou El Battari , Dominique Lombardo

DOI: 10.1016/S0076-6879(97)84022-0

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摘要: Publisher Summary Despite enormous advances due to recombinant DNA techniques, the understanding of complex function protein glycosylation remains primitive. The role glycans on glycoproteins may be threefold. First, glycan participate in folding and influence its stability. Second, not directly associated with glycoprotein but modulate half-life by, for example, favoring or inhibiting hepatic clearance. Third, have biological through interaction target molecules such as homing lymphocytes via selectins. N-linked bile salt-dependent lipase (BSDL) seems important secretion BSDL, further processing structure did affect activity enzyme. Consequently expression BSDL baculovirus-infected Sf9 insect cells appeared appropriate high-level production crystallization

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