Selective proteolysis of abnormal proteins of shortened chain length in rabbit reticulocytes.
Proteolysis of certain shortened globin chains can proceed in cell-free extracts of rabbit reticulocytes in the absence of ATP. Proteolysis of amino acid analogue-induced abnormal globin chains of normal chain length may be stimulated by ATP, however. The ATP independent degradation of globin cyanogen bromide-peptides appears to require the presence of free, unblocked amino groups in the substrate, has a pH optimum of 7.8 and is inhibited by phenanthroline, cobalt and zinc ions, N-ethylmaleimide and cystamine.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002474:Cell-Free System; D055598:Chemical Phenomena; D002621:Chemistry; D003488:Cyanogen Bromide; D003545:Cysteine / Q000031:analogs & derivatives / Q000378:metabolism; D005914:Globins / Q000378:metabolism*; D046911:Macromolecular Substances; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D011691:Puromycin / Q000378:metabolism; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D046911:Macromolecular Substances; D010455:Peptides; C000204:S-2-aminoethyl cysteine; D011691:Puromycin; D000255:Adenosine Triphosphate; D005914:Globins; D010447:Peptide Hydrolases; D003545:Cysteine; D003488:Cyanogen Bromide