Oligomerization of pro-opiomelanocortin is independent of pH, calcium and the sorting signal for the regulated secretory pathway

FEBS Letters

Volumn 481, Issue 1, 2000, Pages 37-41

  Cawley, Niamh X ^a   Normant, Emmanuel ^a   Chen, Anthony ^a   Loh, Y Peng ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

Author keywords

Aggregation; Oligomerization; Pro opiomelanocortin; Prohormone sorting

Indexed keywords

CALCIUM; HORMONE PRECURSOR; PROOPIOMELANOCORTIN;

ANIMAL CELL; CONFERENCE PAPER; CONTROLLED STUDY; FAST PROTEIN LIQUID CHROMATOGRAPHY; IMMUNOBLOTTING; NONHUMAN; OLIGOMERIZATION; PH; PRIORITY JOURNAL; SECRETORY GRANULE; SIGNAL DETECTION;

ANIMALS; BIOLOGICAL TRANSPORT; BLOTTING, WESTERN; CALCIUM; CARBOXYPEPTIDASE H; CARBOXYPEPTIDASES; CELL LINE; CHROMATOGRAPHY, GEL; CROSS-LINKING REAGENTS; HYDROGEN-ION CONCENTRATION; MOLECULAR WEIGHT; PRO-OPIOMELANOCORTIN; PROTEIN BINDING; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE DELETION; SPODOPTERA; TRANSFECTION;

EID: 0034623357     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(00)01961-X     Document Type: Article

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