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Chemico-Biological Interactions|June 1, 1993
Studies on human serum paraoxonase/arylesteraseB N La Du, S Adkins, C L Kuo, et al.Drug Metabolism and Disposition: the Biological Fate of Chemicals|September 1, 1995
Comparison of purified human and rabbit serum paraoxonasesC L Kuo, B N La DuDrug Metabolism and Disposition: the Biological Fate of Chemicals|July 14, 1998
Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymatic activityC L Kuo, B N La DuThe Journal of Biological Chemistry|September 25, 1987
Location of disulfide bonds within the sequence of human serum cholinesteraseO Lockridge, S Adkins, B N La DuProceedings of the National Academy of Sciences of the United States of America|August 1, 1995
Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesteraseR C Sorenson, S L Primo-Parmo, C L Kuo, et al.Progress in Clinical and Biological Research|January 1, 1986
Analysis of the serum paraoxonase/arylesterase polymorphism in some Sudanese familiesB N La Du, S Adkins, R A BayoumiAmerican Journal of Human Genetics|March 1, 1993
Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymesS Adkins, K N Gan, M Mody, et al.Federation Proceedings|December 1, 1986
Molecular biology of human serum cholinesteraseB N La Du, O LockridgeBiochemical Genetics|June 1, 1986
Amino acid sequence of the active site of human serum cholinesterase from usual, atypical, and atypical-silent genotypesO Lockridge, B N La DuPageof 22