Literature DB >> 6764537

Isolation of yeast nuclei. Evidence of chromatin-associated proteolytic activity.

S Ruggieri, G Magni.   

Abstract

Purified yeast nuclei contain proteolytic activities which are associated with chromatin. pH optimum is in the range 8.0--8.5. Partial purification reveals the presence of three fractions corresponding to different molecular weights. Boiled chromatin supernatants are able to inhibit proteolytic activity. The inhibition effect of various compounds is also described. The purity of the chromatin preparation seems to rule out artifacts due to contamination.

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Year:  1982        PMID: 6764537

Source DB:  PubMed          Journal:  Physiol Chem Phys        ISSN: 0031-9325


  3 in total

1.  Recent observations on the structure and the properties of yeast NMN adenylyltransferase.

Authors:  S Ruggieri; L Gregori; P Natalini; A Vita; G Magni
Journal:  Experientia       Date:  1988-01-15

2.  The subnuclear localization of tRNA ligase in yeast.

Authors:  M W Clark; J Abelson
Journal:  J Cell Biol       Date:  1987-10       Impact factor: 10.539

3.  Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein.

Authors:  J P Aris; G Blobel
Journal:  J Cell Biol       Date:  1988-07       Impact factor: 10.539

  3 in total

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