Magnetic resonance spectral characterization of the heme active site of Coprinus cinereus peroxidase

Biochemistry ◽  
1989 ◽  
Vol 28 (8) ◽  
pp. 3338-3345 ◽  
Author(s):  
Gudrun S. Lukat ◽  
Kenton R. Rodgers ◽  
Mark N. Jabro ◽  
Harold M. Goff
Keyword(s):  
Magnetic Resonance ◽  
Active Site ◽  
Spectral Characterization ◽  
Coprinus Cinereus ◽  
Coprinus Cinereus Peroxidase

Magnetic resonance spectral characterization of the prostate after radiotherapy

2000 ◽  
Vol 48 (3) ◽  
pp. 314
Author(s):  
C Menard ◽  
T Bezabeh ◽  
L Leboldus ◽  
S Robertson ◽  
C Littman ◽  
...  
Keyword(s):  
Magnetic Resonance ◽  
Spectral Characterization

Resonance Raman Study of the Active Site of Coprinus cinereus Peroxidase

Biochemistry ◽  
1994 ◽  
Vol 33 (51) ◽  
pp. 15425-15432 ◽  
Author(s):  
Giulietta Smulevich ◽  
Alessandro Feis ◽  
Claudia Focardi ◽  
Jeppe Tams ◽  
Karen G. Welinder
Keyword(s):  
Active Site ◽  
Resonance Raman ◽  
Coprinus Cinereus ◽  
Raman Study ◽  
Coprinus Cinereus Peroxidase

Magnetic resonance spectral characterization of tetrathiotungstate adducts with iron(III) porphyrins

1993 ◽  
Vol 32 (7) ◽  
pp. 1304-1305 ◽  
Author(s):  
Yunghee Oh Kim ◽  
Byungho Song ◽  
Harold M. Goff
Keyword(s):  
Magnetic Resonance ◽  
Spectral Characterization

Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding

1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci
Keyword(s):  
Venous Thromboembolism ◽  
Active Site ◽  
Inhibitory Activity ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Molecular Defect ◽  
Affinity Adsorption ◽  
Italian Family ◽  
Crossed Immunoelectrophoresis

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.

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