منابع مشابه
Colonial heterogeneity of Thiobacillus versutus.
In acetate-limited chemostat cultures started with single-colony cultures of Thiobacillus versutus, a mutant appeared after approximately 85 volume changes. The inhomogeneity of the culture was detected by the development of two different types of colonies on agar plates. When a pure culture of the mutant was grown in a chemostat, parent colonies appeared after almost the same period of time. E...
متن کاملEXAFS analysis of the pH dependence of the blue-copper site in amicyanin from Thiobacillus versutus.
The room temperature Cu K-edge EXAFS (extended X-ray absorption fine structure) spectrum of reduced and oxidized amicyanin, the blue copper protein from Thiobacillus versutus, was measured at low and high pH. The data interpretation was partly based on independent NMR evidence for the occurrence of a ligand histidine protonation at low pH (pKa = 6.9) in the reduced protein. In the oxidized prot...
متن کاملCloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus.
The gene that codes for the alpha-subunit of methylamine dehydrogenase from Thiobacillus versutus, madA, was cloned and sequenced. It codes for a protein of 395 amino acids preceded by a leader sequence of 31 amino acids. The derived amino acid sequence was confirmed by partial amino acid sequencing. The start of the mature protein could not be determined by direct sequencing, since the N termi...
متن کاملProperties of phosphoribulokinase from Thiobacillus neapolitanus.
Partially purified preparations of ribulose-5-phosphate kinase (specific activity, 50 to 125 mumoles per min per mg of protein) were employed in a series of kinetic experiments in the presence of several concentrations of H(+), Mg(2+), adenosine triphosphate (ATP), and phosphoenolpyruvate (PEP). The pH optimum of the enzyme was found to be 7.9; at this pH and above, response of the enzyme to va...
متن کاملIsolation of mitochondrial porin from Neurospora crassa.
Mitochondrial porin forms channels in the outer mitochondrial membrane which allows the passage of molecules with diameters up to -20 A [l-6]. We have described the purification of this protein [7] from purified outer membranes by differential extraction with detergents and anionic exchange chromatography. The purified porin displayed an app. Mr of 31 000 as judged by polyacrylamide gel electro...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1989
ISSN: 0378-1097
DOI: 10.1016/0378-1097(89)90238-3