April 1, 1993Journal of Biological ChemistryOpen Access

Binding of lipoprotein lipase to heparin. Identification of five critical residues in two distinct segments of the amino-terminal domain.

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Population

Human lipoprotein lipase (LPL) variant proteins

Comparison

Site-directed mutagenesis replacing basic… vs Wild-type LPL or other variants

Design

Preclinical

Authors

AHAkira HataCross-Cutting Cardiology DRDavid RidingerHeidelberg University SSS. SutherlandUniversité de Montréal

Discussion

Member takes

Implication

Should not change clinical practice; hypothesis-generating for LPL-heparin interactions in metabolic research.

Structured PICO

Population

Human lipoprotein lipase (LPL) variant proteins

Intervention

Site-directed mutagenesis replacing basic residues in three segments (residues 147-151, 279-282, and 292-304) with alanine

Comparator

Wild-type LPL or other variants

Outcome

Binding affinity to heparin-Superose measured by affinity chromatographysurrogate

Five specific basic residues in two distinct segments of the amino-terminal domain of human lipoprotein lipase are critical for its high-affinity binding to heparin.

Cite This Study

Hata et al. (1993) studied this question.

synapsesocial.com/papers/6a82c376409efddc54d4ac92 https://doi.org/10.1016/s0021-9258(18)52896-9

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Binding of lipoprotein lipase to heparin. Identification of five critical residues in two distinct segments of the amino-terminal domain.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Binding of lipoprotein lipase to heparin. Identification of five critical residues in two distinct segments of the amino-terminal domain.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider