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Purification of clathrin assembly protein from rat liver

Title
Purification of clathrin assembly protein from rat liver
Authors
Kim, HLKim, JA
Ewha Authors
김형래
SCOPUS Author ID
김형래scopus
Issue Date
2000
Journal Title
EXPERIMENTAL AND MOLECULAR MEDICINE
ISSN
1226-3613JCR Link
Citation
vol. 32, no. 4, pp. 222 - 226
Keywords
clathrin-coated vesideCALMAP180assembly
Publisher
KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
Indexed
SCI; SCIE; SCOPUS; KCI WOS scopus
Abstract
Recently, the gene encoding clathrin assembly protein of lymphoid myeloid leukemia (CALM), which is homologous to the AP180, was cloned from rat brain, and its expression differential to AP180 was reported (Kim and Lee, 1999). This gene product promotes the polymerization of clathrin into clathrin cage and found to be a regulator in membrane trafficking between intracellular compartments in eukaryotic cells (Kim et al., 2000). In this study, we have purified the CALM protein from clathrin-coated vesicles of rat liver using the monoclonal antibody against the recombinant N-terminal region of the CALM. The coated proteins extracted from the coated vesicle fraction was further purified by multi-step procedures involving gel-filtration and ion-exchange chromatography and SDS-PAGE. The purified protein with an apparent molecular weight of 100 kD promoted the assembly of clathrin triskelia into clathrin cage. In this respect the CALM protein bears a functional resemblance to the AP180 that has been previously described.
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의학전문대학원 > 의학과 > Journal papers
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