Abstract:
:Previous studies have shown that in mammalian cells proteins of large molecular weight are degraded more rapidly than small ones. Evidence is presented here that half-lives of proteins are also related to their isoelectric points. A double-isotope method was used to compare degradative rates of soluble proteins separated by isoelectric focusing. In rat liver, skeletal muscle, kidney, and brain, more rapid rates of catabolism were found for acidic protein fractions than for neutral or basic ones. Acidic proteins also tended to be degraded faster in several mouse tissues. A literature survey confirmed this trend. For 22 proteins from rat liver, a highly significant correlation was found between rates of degradation and isoelectric points (r = 0.824; P less than 0.01). This relationship between isoelectric point and half-life appears to be distinct from that between protein size and half-life.
journal_name
Proc Natl Acad Sci U S Aauthors
Dice JF,Goldberg ALdoi
10.1073/pnas.72.10.3893keywords:
subject
Has Abstractpub_date
1975-10-01 00:00:00pages
3893-7issue
10eissn
0027-8424issn
1091-6490journal_volume
72pub_type
杂志文章abstract::It had long been thought, but never demonstrated, that imino acids are formed in the reactions catalyzed by D- and L-amino acid oxidases (EC 1.4.3.3 and 1.4.3.2). The formation of imino acids is now shown directly by allowing the amino acid oxidase reaction to proceed in the presence of NaBH(4), when the imino acid is...
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