Direct Radiochemical Determination of Lead-210 in Bone

1965 ◽  
Vol 37 (13) ◽  
pp. 1659-1660 ◽  
Author(s):  
Henry G. Petrow ◽  
Arthur. Cover
1977 ◽  
Vol 49 (2) ◽  
pp. 302-306 ◽  
Author(s):  
Claude W. Sill ◽  
Conrad P. Willis

1961 ◽  
Vol 33 (1) ◽  
pp. 39-41 ◽  
Author(s):  
H. V. Weiss ◽  
M. G. Lai

1972 ◽  
Vol 128 (2) ◽  
pp. 229-235 ◽  
Author(s):  
D. C. Shaw ◽  
J. R. E. Wells

Phaseolain, a carboxypeptidase from French-bean leaves, and a partially purified peptidase from baker's yeast are inhibited by reaction with di-isopropyl phosphorofluoridate. Radioactive di-isopropyl [32P]phosphorofluoridate was used to show that the site of reaction is a unique serine residue and that the sequence of amino acids adjacent to the reactive serine is Glu-Ser-Tyr. This sequence is different from those of other ‘serine’ enzymes previously reported and, for phaseolain, represents an unequivocal example of a ‘serine’ carboxypeptidase.


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