Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B

1988 ◽  
Vol 156 (1) ◽  
pp. 445-450 ◽  
Author(s):  
Shiuan Chen ◽  
Walter Weyler
1989 ◽  
Vol 260 (3) ◽  
pp. 725-729 ◽  
Author(s):  
W Weyler

I present the first clear evidence that the protein: FAD ratio in human monoamine oxidase A and bovine monoamine oxidase B has an upper limit of 65 kDa and 57 kDa per FAD, respectively. To now it had been assumed that the protein: FAD ratio was 100-120 kDa to 1 FAD and that there was one FAD per two subunits which were assumed to be of the same size. For the present work the purity of monoamine oxidase A and monoamine oxidase B was improved over that previously achieved. Protein was determined by quantitative amino acid analysis and FAD content was measured by spectrophotometric titration of SDS-denatured enzyme with NaS2O4 standardized against riboflavin. The cause of the previous misassignment of the protein: FAD ratio was judged as having been due to the use of impure enzyme preparations. Knowledge of the correct protein: FAD ratio is important in devising cloning strategies for this enzyme, in understanding its structure, function, mechanism, and in the studies of its biosynthesis.


FEBS Letters ◽  
1989 ◽  
Vol 247 (2) ◽  
pp. 279-282 ◽  
Author(s):  
Vijay Chhajlani ◽  
Dwight Derr ◽  
Betty Earles ◽  
Eli Schmell ◽  
Thomas August

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