Today's Hours: 8:00am - 10:00pm
Lane Medical Library

Search

Filter Results

Did You Mean:

Search Results

Sort by
relevance
  • Journal
    Digital Access TandFonline v. 1-v. 39, no. 2, 1958-96.
    Print Access Request
    Location
    Version
    Call Number
    Items
    Periodicals (Downstairs)
    v. 1-51, [52], 1958-2009, [2010].
    46
  • Article
    Irie M, Ohgi K, Iwama M.
    J Biochem. 1977 Dec;82(6):1701-6.
    In order to investigate the nature of amino acid residues involved in the active in the active site of a ribonuclease from Aspergillus saitoi, the pH dependence of the rates of inactivation of RNase Ms by photooxidation and modification with diethylpyrocarbonate were studied. (1) RNase Ms was inactivated by illumination in the presence of methylene blue at various pH's. The pH dependence of the rate of photooxidative inactivation of RNase Ms indicated that at least one functional group having pKa 7.2 was involved in the active site. (2) Amino acid analyses of photooxidized RNase Ms at various stages of photooxidative inactivation at pH's 4.0 and 6.0 indicated that one histidine residue was related to the activity of RNase Ms, but that no tryptophan residue was involved in the active site. (3) 2',(3')-AMP prevented the photooxidative inactivation of RNase Ms. The results also indicated the presence of a histidine residue in the active site. (4) Modification of RNase Ms with diethylpyrocarbonate was studied at various pH's. The results indicated that a functional group having pKa 7.1 was involved in the active site of RNase Ms.
    Digital Access Access Options