Search PubMed⌕ Search

Biomedical subjects

S Shaltiel

Publications and source records attributed to S Shaltiel.

At least 73 records · Page 4Linked to original sources
PubMed1976

Resolution and purification of histones on homologous series of hydrocarbon-coated agaroses.

Hydrophobic chromatography on alkyl-agarose columns has been applied to the fractionation of histones. This paper describes: (a) a two-column method for the resolution of whole histone from calf thymus into its five main components (H1, H2a, H2b, H3 and H4), (b) a rapid one-step procedure for the isolation of the H3 fraction from whole histone, (c) an alternative one-step procedure for the resolution of H3 and H2a (which co-elute during gel exclusion chromatography on Biogel P-60). These experiments are also used for gaining further insight into the mechanism of action of hydrocarbon-coated agaroses.

Animals↗
PubMed1975

Omega-aminoalkyl agaroses in the resolution of enzymes involved in regulation of glutamine metabolism.

Systematic examination of a homologous series of omega-aminoalkyl agaroses showed that the pentyl derivative (Seph-C5-NH2) was best suited for the retention and subsequent separation of several proteins involved in the regulation of glutamine metabolism in Escherichia coli, including: glutamine synthetase [EC 6.3.1.2; L-glutamate:ammonia ligase (ADP-forming)], ATP:glutamine synthetase adenylyltransferase (EC 2.7.7.42), the PII regulatory protein which regulates the adenylylation and deadenylylation activities of the adenylyltransferase, the UTP:PII protein uridylyltransferase, and the uridylyl removing enzyme which catalyzes the removal of uridylyl groups from uridylylated PII protein. Resolution of these proteins was achieved by gradually increasing the concentration of KCl in the eluant, which resulted in consecutive detachment of the proteins from the column. Proteins that co-elute from a DEAE-cellulose column can be resolved and further purified on epsilon-aminopentyl agarose, probably due to the fact that with the homologous series it is possible to adjust the contribution of hydrophobic interactions for optimal resolution.

ATP Phosphoribosyltransferase↗
PubMed1973

Hydrophobic chromatography: use for purification of glycogen synthetase.

A homologous series of omega-aminoalkylagaroses [Sepharose-NH(CH(2))(n)NH(2)] that varied in the length of their hydrocarbon side chains was synthesized. This family of agaroses was used for a new type of chromatography, in which retention of proteins is achieved mainly through lipophilic interactions between the hydrocarbon side chains on the agarose and accessible hydrophobic pockets in the protein. When an extract of rabbit muscle was subjected to chromatography on these modified agaroses, the columns with short "arms" (n = 2 and n = 3) excluded glycogen synthetase (EC 2.4.1.11), but the enzyme was retained on delta-aminobutyl-agarose (n = 4), from which it could be eluted with a linear NaCl gradient. Higher members of this series (e.g., n = 6) bind the synthetase so tightly that it can be eluted only in a denatured form. A column of delta-aminobutyl-agarose, which retained the synthetase, excluded glycogen phosphorylase (EC 2.4.1.1), which in this column series and under the same conditions requires side chains 5-(or 6)-carbon-atoms long for retention. Therefore, it is possible to isolate glycogen synthetase by passage of muscle extract through delta-aminobutyl-agarose, then to extract phosphorylase by subjecting the excluded proteins to chromatography on omega-aminohexyl-agarose (n = 6). On a preparative scale, the synthetase (I form) was purified 25- to 50-fold in one step. This paper describes some basic features and potential uses of hydrophobic chromatography. The relevance of the results presented here to the design and use of affinity chromatography columns is discussed.

Animals↗