Isolation and partial characterization of amphibian tyrosine oxidase polysomes

Autor:	E. L. Triplett, L. P. Russell, R. Herzog
Rok vydání:	1970
Předmět:	chemistry.chemical_classification Oxidase test education.field_of_study Sucrose Population Biology Molecular biology Trypsinization Amino acid chemistry.chemical_compound chemistry Biochemistry Polysome Protein biosynthesis Tyrosine education Molecular Biology Developmental Biology
Zdroj:	Development. 24:109-118
ISSN:	1477-9129 0950-1991
DOI:	10.1242/dev.24.1.109
Popis:	A population of polysomes isolated from frog skin is capable of supporting protein synthesis in a cell-free system containing an energy generating system, ‘soluble components and amino acids. These polysomes catalyse the oxidation of DOPA after gentle trypsinization, and they also have antigenic determinants attributable to tyrosine oxidase. Skin polysomes sedimented in 10–30% sucrose gradients contain tyrosine oxidase peaks of enzymic activity at the bottom and top of the tube and in the 250 S regions. A peak of tyrosine oxidase antigenic acitvity is found in the 250–350S region of the gradient. Polysomes resolved on the gradient retain the ability to support protein synthesis in a cell-free system. All 250–350 S particles capable of supporting the incorporation of [14C]amino acid into tyrosine oxidase are precipitable with tyrosine oxidase antibodies. It is probable that 25O–35OS tyrosine oxidase antibody precipitates contain only polysomes for this protein.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::ebb863a887ece992471de1f09bf43787 https://doi.org/10.1242/dev.24.1.109 Zobrazit plný text záznamu