Rapid Purification of Mitochondrial Hexokinase from Rat Brain by a Single Affinity Chromatography Step on Affi-Gel Blue

1989 ◽  
Vol 19 (1) ◽  
pp. 13-21 ◽  
Author(s):  
John E. Wilson
Keyword(s):  
Affinity Chromatography ◽  
Rat Brain ◽  
Rapid Purification ◽  
Chromatography Step

Yeast Aminopeptidase II: Rapid Purification Using Affinity Chromatography of the Periplasmic Enzyme

1982 ◽  
Vol 37 (9) ◽  
pp. 845-848 ◽  
Author(s):  
Joseph Knüver ◽  
Klaus-Heinrich Röhm
Keyword(s):  
Affinity Chromatography ◽  
Ammonium Sulfate ◽  
Isolation Method ◽  
Yeast Protein ◽  
Rapid Purification ◽  
Periplasmic Enzyme

Periplasmic aminopeptidase II of yeast was isolated from protoplast supernatants by ammonium sulfate precipita­tion, DEAE-Sephacel chromatography and affinity chromatography on immobilized bestatin. This isolation method is more rapid than conventional procedures and, in addition, avoids contact of the enzyme with yeast protein-ases. Thus the preparation obtained is likely to represent the native periplasmic from of aminopeptidase II.

Development and validation of an affinity chromatography step using a peptide ligand for cGMP production of factor VIII

2004 ◽  
Vol 87 (3) ◽  
pp. 400-412 ◽  
Author(s):  
Brian D. Kelley ◽  
Molly Tannatt ◽  
Robert Magnusson ◽  
Sigrid Hagelberg ◽  
James Booth
Keyword(s):  
Factor Viii ◽  
Affinity Chromatography ◽  
Peptide Ligand ◽  
Cgmp Production ◽  
Development And Validation ◽  
Chromatography Step

scholarly journals Purification to homogeneity of an active opioid receptor from rat brain by affinity chromatography.

1994 ◽  
Vol 91 (10) ◽  
pp. 4574-4578 ◽  
Author(s):  
S. Loukas ◽  
M. Mercouris ◽  
F. Panetsos ◽  
C. Zioudrou
Keyword(s):  
Affinity Chromatography ◽  
Rat Brain ◽  
Opioid Receptor

Identification of Renin and Renin-like Enzymes in Rat Brain by a Renin-Specific Antibody

1980 ◽  
Vol 59 (s6) ◽  
pp. 45s-47s ◽  
Author(s):  
V. J. Dzau ◽  
Amy Brenner ◽  
Neremiah Emmett ◽  
E. Haber
Keyword(s):  
Affinity Chromatography ◽  
Rat Brain ◽  
Specific Antibody ◽  
Angiotensin I ◽  
Ph Optimum ◽  
Brain Extracts ◽  
Antibody Inhibition ◽  
Neutral Proteases

1. The major angiotensin I-generating activity of rat brain extracts has a pH optimum different from that of renal renin and is not inhibited by renin specific antibody. 2. Affinity chromatography utilizing renin specific antibody, pepstatin and α-casein yielded fractions that resembled renal renin more closely with respect to antibody inhibition and pH optimum as well as an absence of the ability to hydrolyse haemoglobin. 3. We conclude that rat brain contains a host of enzymes with angiotensin I-generating activity including acid and neutral proteases and an enzyme with the immunochemical identity of renal renin. The biosynthetic origins of this renin-like protein remain uncertain.

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