Isolation and characterization of an active-site peptide from triose phosphate isomerase

1970 ◽  
Vol 92 (7) ◽  
pp. 2170-2172 ◽  
Author(s):  
Fred C. Hartman
Biochemistry ◽  
1970 ◽  
Vol 9 (25) ◽  
pp. 4952-4958 ◽  
Author(s):  
Fred C. Hartman ◽  
I. L. Norton ◽  
Peter Pfuderer ◽  
C. D. Stringer

1984 ◽  
Vol 218 (1) ◽  
pp. 113-118 ◽  
Author(s):  
A J Balmforth ◽  
A Thomson

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.


Biochemistry ◽  
1988 ◽  
Vol 27 (26) ◽  
pp. 9093-9101 ◽  
Author(s):  
Walter E. DeWolf ◽  
Steven A. Carr ◽  
Angela Varrichio ◽  
Paula J. Goodhart ◽  
Mary A. Mentzer ◽  
...  

Nature ◽  
1970 ◽  
Vol 227 (5254) ◽  
pp. 180-181 ◽  
Author(s):  
A. F. W. COULSON ◽  
J. R. KNOWLES ◽  
J. D. PRIDDLE ◽  
R. E. OFFORD

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