Zobrazeno 1 - 10
of 11
pro vyhledávání: '"M. O. Funk"'
Publikováno v:
International Journal of Peptide and Protein Research. 13:296-303
The reinvestigation of the affinity chromatographic method of purifying papain has been carried out. It has been reported that papain could be purified by taking advantage of the affinity of the enzyme for the insolubilized peptide inhibitor, agarose
Publikováno v:
Proteins. 29(1)
Soybean lipoxygenase isoenzyme L3 represents a second example (after L1) of the X-ray structure (R = 17% at 2.6 A resolution) for a member of the large family of lipoxygenases. L1 and L3 have different characteristics in catalysis, although they shar
Publikováno v:
Biochemistry. 31(33)
Soybean lipoxygenase 1 was studied using limited proteolysis and active-site labeling to begin the structural characterization of the enzyme in solution. The serine proteases trypsin and chymotrypsin cleaved the large monomeric protein (95 kDa) into
Hydrolysis of 1-benzyl-3-bromoacetylpyridinium bromide. Evidence for neighboring group participation
Autor:
M. O. Funk, E. T. Kaiser
Publikováno v:
Journal of the American Chemical Society. 99:5336-5340
Publikováno v:
Chemischer Informationsdienst. 16
Autor:
N. A. PORTER, M. O. FUNK
Publikováno v:
Chemischer Informationsdienst. 7
Publikováno v:
International journal of peptide and protein research. 13(3)
The reinvestigation of the affinity chromatographic method of purifying papain has been carried out. It has been reported that papain could be purified by taking advantage of the affinity of the enzyme for the insolubilized peptide inhibitor, agarose
Publikováno v:
Chemischer Informationsdienst. 13
Autor:
M. O. FUNK, E. T. KAISER
Publikováno v:
Chemischer Informationsdienst. 8
Publikováno v:
Journal of the American Chemical Society. 97(5)