scholarly journals Inactivation of Rabbit Muscle Adenosine Triphosphate-Adenosine 5'-Phosphate Phosphotransferase by Alkylation of Methionine Residues

1967 ◽  
Vol 242 (4) ◽  
pp. 558-564
Author(s):  
Lawrence F. Kress ◽  
L. Noda
1971 ◽  
Vol 122 (2) ◽  
pp. 209-218 ◽  
Author(s):  
Janet C. Miller ◽  
S. G. Waley

1. The nature of the subunits in rabbit muscle triose phosphate isomerase has been investigated. 2. Amino acid analyses show that there are five cysteine residues and two methionine residues/subunit. 3. The amino acid sequences around the cysteine residues have been determined; these account for about 75 residues. 4. Cleavage at the methionine residues with cyanogen bromide gave three fragments. 5. These results show that the subunits correspond to polypeptide chains, containing about 230 amino acid residues. The chains in triose phosphate isomerase seem to be shorter than those of other glycolytic enzymes.


Biochemistry ◽  
1974 ◽  
Vol 13 (13) ◽  
pp. 2683-2688 ◽  
Author(s):  
M. M. Werber ◽  
A. Oplatka ◽  
A. Danchin

Biochemistry ◽  
1984 ◽  
Vol 23 (11) ◽  
pp. 2393-2399 ◽  
Author(s):  
Stephen A. Kuby ◽  
Richard H. Palmieri ◽  
Asta Frischat ◽  
Anne H. Fischer ◽  
Lily H. Wu ◽  
...  

1961 ◽  
Vol 39 (7) ◽  
pp. 1133-1140 ◽  
Author(s):  
H. B. Stewart ◽  
K. P. Strickland

A simple method is described for the enzymic preparation of L-α-glycerophosphate from hexose diphosphate or from glucose and adenosine triphosphate. The necessary enzymes are supplied by a glycolyzing preparation from yeast supplemented with rabbit muscle L-a-glycerophosphate dehydrogenase. The method has been adapted to the preparation of carbon- and phosphorus-labelled products by using glucose-U-C14and adenosine-triphosphate-P32as precursors.


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