scholarly journals Linkage of an acetylenic secosteroid suicide substrate to the active site of delta 5-3-ketosteroid isomerase. Isolation and characterization of a tetrapeptide.

1981 ◽  
Vol 256 (13) ◽  
pp. 6851-6858
Author(s):  
T.M. Penning ◽  
P. Talalay
Keyword(s):  
Active Site ◽  
Ketosteroid Isomerase ◽  
Isolation And Characterization ◽  
Suicide Substrate

scholarly journals Isolation and characterization of glyoxylate dehydrogenase from the fungus Sclerotium rolfsii

1984 ◽  
Vol 218 (1) ◽  
pp. 113-118 ◽  
Author(s):  
A J Balmforth ◽  
A Thomson
Keyword(s):  
Affinity Chromatography ◽  
Active Site ◽  
Sclerotium Rolfsii ◽  
Thiol Group ◽  
Isolation And Characterization ◽  
Crude Extracts ◽  
Nad Oxidoreductase ◽  
Inhibition Studies ◽  
Dye Affinity Chromatography

Glyoxylate dehydrogenase (glyoxylate: NAD+ oxidoreductase) was purified 600-fold in three steps from crude extracts of the fungus Sclerotium rolfsii (Corticium rolfsii Curzi). Two of the purification steps involved dye-affinity chromatography. The enzyme is a tetramer of Mr 250 000, with identical subunits of Mr 57 000. Inhibition studies suggest that there is one essential thiol group per active site.

Inactivation of dopamine .beta.-hydroxylase by p-cresol: isolation and characterization of covalently modified active site peptides

Biochemistry ◽  
1988 ◽  
Vol 27 (26) ◽  
pp. 9093-9101 ◽  
Author(s):  
Walter E. DeWolf ◽  
Steven A. Carr ◽  
Angela Varrichio ◽  
Paula J. Goodhart ◽  
Mary A. Mentzer ◽  
...  
Keyword(s):  
Active Site ◽  
Isolation And Characterization ◽  
Dopamine Beta Hydroxylase

The isolation and characterization of active site peptides in lysyl oxidase

1997 ◽  
pp. 351-361
Author(s):  
Sophie X. Wang ◽  
Judith P. Klinman ◽  
Katalin F. Medzihradszky ◽  
Alma L. Burlingame
Keyword(s):  
Active Site ◽  
Lysyl Oxidase ◽  
Isolation And Characterization

scholarly journals Isolation and characterization of conformation sensitive antierythropoietin monoclonal antibodies: effect of disulfide bonds and carbohydrate on recombinant human erythropoietin structure

Blood ◽  
1996 ◽  
Vol 87 (7) ◽  
pp. 2714-2722 ◽  
Author(s):  
S Elliott ◽  
D Chang ◽  
E Delorme ◽  
C Dunn ◽  
J Egrie ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Active Site ◽  
Disulfide Bonds ◽  
Recombinant Human Erythropoietin ◽  
Human Erythropoietin ◽  
Isolation And Characterization

We have isolated and characterized three anti-recombinant human erythropoietin (rHuEPO) monoclonal antibodies (MoAbs) that recognize nonoverlapping epitopes on rHuEPO. Anti-EPO MoAb D11 neutralizes rHuEPO activity whereas MoAbs F12 and 9G8A do not. This suggests that D11 may bind to the rHuEPO active site. MoAbs F12 and D11 recognize conformation dependent epitopes whereas 9G8A does not. Immunoassays were developed for each monoclonal. The 9G8A immunoassay was novel and useful because immunoreactivity increased when rHuEPO was denatured. Disruption of disulfide bonds or removal of carbohydrate increased 9G8A immunoreactivity, which suggests that these elements are important for rHuEPO structure or stability.

Amino acid sequence of penicillopepsin. II. Isolation and characterization of thermolytic peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 885-894 ◽  
Author(s):  
Leticia Rao ◽  
Theo Hofmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Amino Acid Sequences ◽  
Porcine Pepsin ◽  
Isolation And Characterization

The determination of the amino acid sequences of 70 peptides obtained from a thermoiytic digest of penicillopepsin (EC 3.4.23.7) is described. Fifty-six unique sequences ranging from 2 to 13 amino acids were compiled. Among these was a heptapeptide whose sequence is nearly identical with that of the epoxide-reactive active site peptide of porcine pepsin (EC 3.4.23.1). Considering unrecognized overlaps, a minimum of 272 and a maximum of 293 unique amino acids have been obtained. They account for about 90% of the amino acids of the enzyme.

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