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Journal of Biochemistry
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January 1, 1992
Studies on the active site of human alpha-amylases: examination of the third subsite S3' of the aglycone-binding site by control of substrate binding mode
K Omichi, S Hase, T Ikenaka
Journal of Biochemistry
|
September 1, 1972
Studies on the substrate specificity of Taka-amylase A. X. Change in the mode of substrate binding by p-phenylazobenzoylation of the enzyme
K Omichi, T Ikenaka, Y Matsushima
The International Journal of Biochemistry
|
January 1, 1983
Preparation of neuraminidase-resistant human alpha 1-protease inhibitor and its clearance in rat blood circulation
K Omichi, G Savic, A Yoshida
Journal of Biochemistry
|
September 1, 1975
Studies on the substrate specificity of Taka-amylase A. XII. Investigation of the active site of Taka-amylase A by examining the properties of p-phenylazobenzoyl Taka-amylase A
K Omichi, S Kasai, Y Matsushima
Journal of Biochemistry
|
April 1, 1982
Purification and characterization of protease inhibitors from peanuts (Arachis hypogaea)
S Norioka, K Omichi, T Ikenaka
Journal of Biochemistry
|
March 1, 1991
Examination of aglycone-binding site of human salivary alpha-amylase by means of transglycosylation reactions
K Omichi, S Hase, T Ikenaka
Journal of Biochemistry
|
September 1, 1988
Investigation of the active site of human salivary alpha-amylase from the modes of action on modified maltooligosaccharides
Y Nagamine, K Omichi, T Ikenaka
Journal of Biochemistry
|
February 1, 1980
The reactive site of Streptomyces subtilisin inhibitor
K Omichi, N Nagura, T Ikenaka
Journal of Biochemistry
|
October 1, 1987
Studies on the active site of Taka-amylase A: its action on phenyl maltooligosides with a charge at their non-reducing-ends
Y Nagamine, M Sumikawa, K Omichi, et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry
|
June 15, 1988
Alpha-amylase assay with use of a benzyl derivative of p-nitrophenyl alpha-maltopentaoside, BG5P
S Satomura, Y Sakata, K Omichi, et al.
Page
of 6
Search research articles
Search
Showing results (31-40 of 60) with videos related to
Sort By:
Page
of 6
Journal of Biochemistry
|
January 1, 1992
Studies on the active site of human alpha-amylases: examination of the third subsite S3' of the aglycone-binding site by control of substrate binding mode
K Omichi, S Hase, T Ikenaka
Journal of Biochemistry
|
September 1, 1972
Studies on the substrate specificity of Taka-amylase A. X. Change in the mode of substrate binding by p-phenylazobenzoylation of the enzyme
K Omichi, T Ikenaka, Y Matsushima
The International Journal of Biochemistry
|
January 1, 1983
Preparation of neuraminidase-resistant human alpha 1-protease inhibitor and its clearance in rat blood circulation
K Omichi, G Savic, A Yoshida
Journal of Biochemistry
|
September 1, 1975
Studies on the substrate specificity of Taka-amylase A. XII. Investigation of the active site of Taka-amylase A by examining the properties of p-phenylazobenzoyl Taka-amylase A
K Omichi, S Kasai, Y Matsushima
Journal of Biochemistry
|
April 1, 1982
Purification and characterization of protease inhibitors from peanuts (Arachis hypogaea)
S Norioka, K Omichi, T Ikenaka
Journal of Biochemistry
|
March 1, 1991
Examination of aglycone-binding site of human salivary alpha-amylase by means of transglycosylation reactions
K Omichi, S Hase, T Ikenaka
Journal of Biochemistry
|
September 1, 1988
Investigation of the active site of human salivary alpha-amylase from the modes of action on modified maltooligosaccharides
Y Nagamine, K Omichi, T Ikenaka
Journal of Biochemistry
|
February 1, 1980
The reactive site of Streptomyces subtilisin inhibitor
K Omichi, N Nagura, T Ikenaka
Journal of Biochemistry
|
October 1, 1987
Studies on the active site of Taka-amylase A: its action on phenyl maltooligosides with a charge at their non-reducing-ends
Y Nagamine, M Sumikawa, K Omichi, et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry
|
June 15, 1988
Alpha-amylase assay with use of a benzyl derivative of p-nitrophenyl alpha-maltopentaoside, BG5P
S Satomura, Y Sakata, K Omichi, et al.
Page
of 6