246 results found
Freemont PS, Ollis DL, Steitz TA, et al., 1986, A domain of the Klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity., Proteins, Vol: 1, Pages: 66-73, ISSN: 0887-3585
The Klenow fragment of DNA polymerase I from Escherichia coli has two enzymatic activities: DNA polymerase and 3'-5' exonuclease. The crystal structure showed that the fragment is folded into two distinct domains. The smaller domain has a binding site for deoxynucleoside monophosphate and a divalent metal ion that is thought to identify the 3'-5' exonuclease active site. The larger C-terminal domain contains a deep cleft that is believed to bind duplex DNA. Several lines of evidence suggested that the large domain also contains the polymerase active site. To test this hypothesis, we have cloned the DNA coding for the large domain into an expression system and purified the protein product. We find that the C-terminal domain has polymerase activity (albeit at a lower specific activity than the native Klenow fragment) but no measurable 3'-5' exonuclease activity. These data are consistent with the hypothesis that each of the three enzymatic activities of DNA polymerase I from E. coli resides on a separate protein structural domain.
STEITZ TA, FREEMONT PS, OLLIS DL, et al., 1986, FUNCTIONAL IMPLICATIONS OF THE KLENOW FRAGMENT STRUCTURE, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 14, Pages: 205-207, ISSN: 0300-5127
STEITZ TA, FREEMONT PS, JOYCE CM, 1986, SOME FUNCTIONAL IMPLICATIONS OF THE STRUCTURE OF THE KLENOW FRAGMENT, JOURNAL OF CELLULAR BIOCHEMISTRY, Pages: 126-126, ISSN: 0730-2312
FREEMONT PS, DUNBAR B, FOTHERGILL LA, 1984, HUMAN SKELETAL-MUSCLE ALDOLASE - N-TERMINAL SEQUENCE-ANALYSIS OF CNBR-IODOSOBENZOIC AND ORTHO-IODOSOBENZOIC ACID CLEAVAGE FRAGMENTS, ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, Vol: 228, Pages: 342-352, ISSN: 0003-9861
Freemont PS, Dunbar B, Fothergill LA, 1984, Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments., Arch Biochem Biophys, Vol: 228, Pages: 342-352, ISSN: 0003-9861
Fructose-1,6-bisphosphate aldolase was purified from human skeletal-muscle by affinity elution chromatography. Four CNBr-cleavage fragments were purified by gel filtration, and their N-terminal amino acid sequences were determined. Cleavage with o-iodosobenzoic acid at the three tryptophan residues also yielded fragments suitable for N-terminal sequence analysis. Thus, the sequence of 272 of the 363 residues was established. These sequence results allow many of the discrepancies between the two published rabbit skeletal-muscle aldolase sequences to be resolved. The human aldolase sequence reported here is 96% identical to a "consensus" rabbit aldolase sequence. A comparison with a partial sequence of Drosophila aldolase (103 residues) shows 80% identity. The determination of the amino acid sequence of human aldolase is important for the interpretation of the crystal structure of this enzyme.
BRIGGS CC, FREEMONT PS, LILLEY TH, 1971, EFFECT OF SOLUTES ON SODIUM SULPHATE DECAHYDRATE TRANSITION TEMPERATURE, JOURNAL OF THE CHEMICAL SOCIETY A -INORGANIC PHYSICAL THEORETICAL, Pages: 2603-&
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