Study the effect of trypsin enzyme activity on the screening of applying frontal affinity chromatography

2019 ◽  
Vol 139 ◽  
pp. 740-751
Author(s):  
JunQing Qian ◽  
ChangYan Zhao ◽  
Jun Tong ◽  
ShengLan Jiang ◽  
Zheng Zhang ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Affinity Chromatography ◽  
Frontal Affinity Chromatography

Single-step purification of urease by affinity chromatography

1974 ◽  
Vol 20 (4) ◽  
pp. 623-630 ◽  
Author(s):  
Bassanio L. Wong ◽  
Charles R. Shobe
Keyword(s):  
Enzyme Activity ◽  
Affinity Chromatography ◽  
Single Step ◽  
Jack Bean Urease ◽  
Jack Bean ◽  
Specific Activities ◽  
Single Step Purification

Single-step purification of urease (urea aminohydrolase; EC. 3.5.1.5) from cell-free extracts of Proteus morganii and from partially purified preparations of jack bean urease were achieved in less than 90 min by affinity chromatography on hydroxyurea-substituted beaded agarose columns. The specific activities of the purified enzymes were as high as, or higher than, those reported by other authors for urease preparations obtained by conventional techniques. In addition, yields of enzyme activity were routinely 6 to 100 times greater than recoveries previously reported for this enzyme.

scholarly journals Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography

Glycobiology ◽  
2005 ◽  
Vol 16 (1) ◽  
pp. 46-53 ◽  
Author(s):  
Kouichi Tachibana ◽  
Sachiko Nakamura ◽  
Han Wang ◽  
Hiroko Iwasaki ◽  
Kahori Tachibana ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Affinity Chromatography ◽  
Binding Specificity ◽  
Frontal Affinity Chromatography

scholarly journals Identification of rat liver phosphatidylinositol synthase as a 21 kDa protein

1994 ◽  
Vol 304 (1) ◽  
pp. 301-305 ◽  
Author(s):  
M E Monaco ◽  
M Feldman ◽  
D L Kleinberg
Keyword(s):  
Heat Treatment ◽  
Enzyme Activity ◽  
Affinity Chromatography ◽  
Molecular Mass ◽  
Rat Liver ◽  
Protein Band ◽  
Absolute Requirement ◽  
Sds Page ◽  
Sepharose 4B ◽  
Post Mitochondrial Supernatant

Substantial purification of rat liver phosphatidylinositol (PtdIns) synthase has been achieved by a combination of Hecameg extraction, heat treatment, affinity chromatography and chromatography on PBE-94. The activity chromatographs as a single peak which has an apparent molecular mass between 150 and 200 kDa on Sepharose 4B. When analysed by SDS/PAGE, two major bands are seen. The enzyme activity is correlated with a protein band of 21 kDa. A second band, at 51 kDa, is eluted from a PBE-94 column slightly ahead of the activity. Manganese is an absolute requirement for stabilization of activity in the presence of detergent. The effect of manganese is optimal at 0.5 mM; magnesium at a concentration of 10 mM is only minimally effective. Substrate Kms are 1.3 mM and 9.5 microM for inositol and CDP-diacylglycerol respectively. The activity eluting from the PBE-94 column is purified 5000-fold over the post-mitochondrial supernatant.

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