Formation of protein charge ladders by acylation of amino groups on proteins

Journal of the American Chemical Society

Volumn 119, Issue 52, 1997, Pages 12701-12709

  Colton, Ian J ^a   Anderson, Janelle R ^a   Gao, Jinming ^a   Chapman, Robert G ^a   Isaacs, Lyle ^a   Whitesides, George M ^a  

^a HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LACTATE DEHYDROGENASE;

ACYLATION; ARTICLE; CAPILLARY ELECTROPHORESIS; CHEMICAL STRUCTURE; ELECTROPHORETIC MOBILITY; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE; PH; PROTEIN STRUCTURE;

EID: 0031593107     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9723491     Document Type: Article

References (9)

1. For an early example of a charge ladder, see: Creighton, T. E. Nature 1980, 284, 487-489.
2. Allison, S. A.; Potter, M.; McCammon, J. A. Biophys. J. 1997, 73, 133-140.
3. Aviram, I.; Myer, Y. P.; Schejter, A. J. Biol. Chem. 1981, 256, 5540-5544.
4. Electroosmotic flow (EOF) is the bulk flow of solution in a capillary that results from the application of an electric field. The value of EOF is typically expressed as the time required for a neutral marker to migrate from the inlet of a capillary to the detector window.
5. CE and/or coefficient of friction for the different regioisomers that make up these rungs.
6. Nozaki, Y.; Tanford, C. Methods Enzymol. 1967, 11, 715-734.
7. Ford, C. L.; Winzor, D. J. Biochim. Biophys. Acta 1982, 703, 109-112.
8. Öjteg, G.; Lundahl, P.; Wolgast, M. Biochim. Biophys. Acta 1989, 991, 317-323.
9. We did not include certain commercial proteins that gave ambiguous results upon acylation. Native hexokinase and pancreatic lipase from Worthington and hemoglobin from Sigma revealed multiple peaks by CE. The impurities present in these samples made assignment of the some of the rungs of the charge ladders of these proteins difficult due to the overlapping of peaks.