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Toxicon : Official Journal of the International Society on Toxinology|January 1, 1988
Separation and characterization of four different amino acid sequence variants of a sea anemone (Stichodactyla helianthus) protein cytolysinW R Kem, B M DunnThe Journal of Biological Chemistry|June 28, 1996
Self-activation of recombinant human lysosomal procathepsin D at a newly engineered cleavage junction, "short" pseudocathepsin DB M Beyer, B M DunnBiochemistry|June 3, 1975
Evaluation of quantitative affinity chromatography by comparison with kinetic and equilibrium dialysis methods for the analysis of nucleotide binding to staphylococcal nucleaseB M Dunn, I M ChaikenProtein Engineering|April 1, 1994
Redesign of the substrate specificity of human cathepsin D: the dominant role of position 287 in the S2 subsiteP E Scarborough, B M DunnProceedings of the National Academy of Sciences of the United States of America|June 1, 1974
Quantitative affinity chromatography. Determination of binding constants by elution with competitive inhibitorsB M Dunn, I M ChaikenProtein Science : a Publication of the Protein Society|March 26, 1998
Prime region subsite specificity characterization of human cathepsin D: the dominant role of position 128B M Beyer, B M DunnTrends in Biochemical Sciences|March 1, 1990
The prediction of transmembrane protein sequences and their conformation: an evaluationG D Fasman, W A GilbertJournal of Biochemistry|October 1, 1996
Substrate specificities of pepstatin-insensitive carboxyl proteinases from gram-negative bacteriaM Ito, B M Dunn, K OdaJournal of Biochemistry|January 9, 1999
Subsite preferences of pepstatin-insensitive carboxyl proteinases from bacteriaS Narutaki, B M Dunn, K OdaBiochimica Et Biophysica Acta|April 8, 1992
Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. No. 101K Oda, H Nakatani, B M DunnPageof 9