Literature DB >> 7055583

The isolation, purification, and properties of a ribonuclease (Mr 18 000) from human uremic serum, and its relation to the human urinary ribonuclease (Mr 33 000). II. Properties of the enzymes.

E Z Rabin, B Tattrie.   

Abstract

A low molecular weight ribonuclease (Mr 18 000) isolated and purified from human uremic serum was found to have similar properties to the high molecular weight ribonuclease (Mr 33 000) isolated from human urine. A detailed comparative study of both enzymes was undertaken to investigate the relationship between them. It is suggested that poly(C)-avid human ribonucleases have similar amino acid compositions but variable carbohydrate contents and that variations in the sugar content are responsible for variations in the molecular weight.

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Year:  1982        PMID: 7055583     DOI: 10.1016/0167-4838(82)90321-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Sequence-specific backbone (1)H, (13)C, and (15)N resonance assignments of human ribonuclease 4.

Authors:  Donald Gagné; Nicolas Doucet
Journal:  Biomol NMR Assign       Date:  2014-07-17       Impact factor: 0.746

2.  Differences in glycosylation pattern of human secretory ribonucleases.

Authors:  J J Beintema; A Blank; G L Schieven; C A Dekker; S Sorrentino; M Libonati
Journal:  Biochem J       Date:  1988-10-15       Impact factor: 3.857

  2 in total

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