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H R Horton

Explore the profile of H R Horton including associated specialties, affiliations and a list of published articles. Areas
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Articles 48
Citations 119
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Recent Articles
1.
Horton H, Koshland Jr D
Methods Enzymol . 2012 Sep; 25:468-82. PMID: 23014428
No abstract available.
2.
Stabel T, Casale E, Swaisgood H, Horton H
Appl Biochem Biotechnol . 1992 Aug; 36(2):87-96. PMID: 1359836
Rabbit anti-bovine IgG was covalently immobilized on thionyl chloride-activated succinamidopropyl controlled-pore glass (CPG) beads (3000 A pore diam; 120/200 mesh). Thionyl chloride-activated beads remained stable for over 1 y retaining...
3.
Clare D, Pinnix I, Lecce J, Horton H
Arch Biochem Biophys . 1988 Sep; 265(2):351-61. PMID: 3048213
Immunofluorescent studies showed that antibodies prepared against bovine milk sulfhydryl oxidase reacted with acinar cells of porcine and bovine pancreas. A close inspection of the specific location within bovine pancreatic...
4.
Koszalka G, Swaisgood H, Horton H
Biochim Biophys Acta . 1987 Sep; 915(2):321-9. PMID: 3115296
The rate of oxidation of glutathione by solubilized sulfhydryl oxidase was significantly enhanced in the presence of horseradish peroxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7). This enhancement was proportional to the amount...
5.
Horton H, Swaisgood H
Methods Enzymol . 1987 Jan; 135:130-41. PMID: 3600296
No abstract available.
6.
Swaisgood H, Horton H
Methods Enzymol . 1987 Jan; 143:504-10. PMID: 3498875
No abstract available.
7.
Song K, Swaisgood H, Horton H
J Dairy Sci . 1986 Oct; 69(10):2589-92. PMID: 3805443
Sulfhydryl oxidase was isolated from bovine skim milk membranes using a transient covalent affinity chromatographic method. This preparation exhibited two chemically reactive sulfhydryl groups in the native enzyme and three...
8.
Duval G, Swaisgood H, Horton H
Biochemistry . 1985 Apr; 24(8):2067-72. PMID: 4016101
Some kinetic characteristics of immobilized native mitochondrial malate dehydrogenase dimers and immobilized protomers, prepared by direct immobilization under conditions yielding complete dissociation without substantial unfolding, were compared to those of...
9.
Schmelzer C, Swaisgood H, Horton H
Biochim Biophys Acta . 1985 Feb; 827(2):140-3. PMID: 3967034
Covalent chromatographically isolated bovine kidney sulfhydryl oxidase was found to catalyze the oxidation of cysteine and cysteine-containing substrates as determined by assaying with 5,5'-dithiobis(2-nitrobenzoate). Monitoring the time-course of substrate disappearance...
10.
Janolino V, Swaisgood H, Horton H
J Appl Biochem . 1985 Feb; 7(1):33-7. PMID: 4008393
During the refolding and oxidation of reductively denatured ribonuclease A in solution, there is a marked lag in appearance of enzymatic activity as compared to the oxidation of sulfhydryl groups,...