Interactions of calcium and other metal ions with caldolysin, the thermostable proteinase from Thermus aquaticus strain T351
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چکیده
منابع مشابه
Thermostable aldolase from Thermus aquaticus.
Data are presented on the purification and properties of the thermostable fructose-1,6-diphosphate aldolase of Thermus aquaticus, a nonsporulating, extreme thermophile. The enzyme shows little activity at temperatures below 60 C and optimal activity at about 95 C. The enzyme was purified 43-fold by diethylaminoethyl cellulose column chromatography and Sephadex G-200 gel filtration. The enzyme i...
متن کاملPurification by affinity chromatography of thermostable glyceraldehyde 3-phosphate dehydrogenase from Thermus aquaticus.
activities of the key enzymes of gluconeogenesis in the liver and kidney of the foetal guinea pig have been followed. The foetal guinea pigs used had a gestational age of 68-72 days. Pyruvate carboxylase was present at very low activities in the kidney of the foetus and neonatal animal and also in the foetal liver until day 50, when it increased in activity to reach a value by day 60 of more th...
متن کاملPurification and some properties of a thermostable metal proteinase produced by Thermomicrobium sp. KN-22 strain.
An extreme thermophile that produces a heat-stable proteinase was isolated from hot-spring water and classified as Thermomicrobium sp. KN-22 (growth temperature, 50-83 degrees C; and optimum growth temperature, 70 degrees C). The proteinase was purified from the culture broth of this strain by fractionation with ammonium sulfate, chromatography on columns of DEAE-cellulose and CM-Sepharose CL-6...
متن کاملamplification and cloning of taq dna polymerase gene from thermus aquaticus strain yt-1
dna amplification using taq dna polymerase is one of the most widely used techniques in molecular biology and biotechnology. the aim of this study was to amplify the gene of this enzyme from a thermophilic bacteria called thermus aqauticus and clone it into a vector for future use. using specific primers the cdna of taq dna polymerase was amplified and ligated into the cloning vector ptz57r usi...
متن کاملOligomerization of a MutS mismatch repair protein from Thermus aquaticus.
The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases. We have examined the oligomerization of a MutS protein from Thermus aquaticus that binds to heteroduplex DNAs at elevated temperatures. Analytical gel filtration, cross-linking of MutS protein with disuccinimidyl suberate, light scattering, and matrix-assisted laser desorption/ionization time-of-f...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1984
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2210407