Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure.
Open Access
- 1 January 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (2) , 1077-1084
- https://doi.org/10.1016/s0021-9258(17)35285-7
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- The interpretation of protein structures: Estimation of static accessibilityPublished by Elsevier ,2004
- Structural features of cartilage matrix protein deduced from cDNA.Proceedings of the National Academy of Sciences, 1987
- Structural characteristics of the PHO8 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiaeGene, 1987
- Amino acid sequence of human von Willebrand factorBiochemistry, 1986
- Nucleotide sequence of the alkaline phosphatase gene of Escherichia coliGene, 1986
- Refined structure of alkaline phosphatase from Escherichia coli at 2.8 Å resolutionJournal of Molecular Biology, 1985
- Determination by cadmium-113 nuclear magnetic resonance of the structural basis for metal ion dependent anticooperativity in alkaline phosphataseBiochemistry, 1980
- Characterization of the properties of the multiple metal binding sites in alkaline phosphatase by carbon-13 nuclear magnetic resonanceBiochemistry, 1980
- Characterization of the histidine residues in alkaline phosphatase by carbon-13 nuclear magnetic resonanceBiochemistry, 1980
- Sporulation in Bacillus subtilis 168. Comparison of alkaline phosphatase from sporulating and vegetative cellsBiochemical Journal, 1971