Skip to main content

. 1961 Dec;47(12):1996–2005. doi: 10.1073/pnas.47.12.1996

PHOSPHATE INCORPORATION INTO ALKALINE PHOSPHATASE OF E. COLI^{^*}

James H Schwartz ¹, Fritz Lipmann ¹

PMCID: PMC223253 PMID: 13909705

2000

Images in this article

Image
on p.1998

Image
on p.1999

Image
on p.2000

Image
on p.2001

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

COHEN J. A., OOSTERBAAN R. A., JANSZ H. S., BERENDS F. The active site of esterases. J Cell Comp Physiol. 1959 Dec;54:231–244. doi: 10.1002/jcp.1030540419. [DOI] [PubMed] [Google Scholar]
ECHOLS H., GAREN A., GAREN S., TORRIANI A. Genetic control of repression of alkaline phosphatase in E. coli. J Mol Biol. 1961 Aug;3:425–438. doi: 10.1016/s0022-2836(61)80055-7. [DOI] [PubMed] [Google Scholar]
GAREN A., LEVINTHAL C. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase. Biochim Biophys Acta. 1960 Mar 11;38:470–483. doi: 10.1016/0006-3002(60)91282-8. [DOI] [PubMed] [Google Scholar]
JONES M. E., SPECTOR L. The pathway of carbonate in the biosynthesis of carbamyl phosphate. J Biol Chem. 1960 Oct;235:2897–2901. [PubMed] [Google Scholar]
KOSHLAND D. E., Jr The active site and enzyme action. Adv Enzymol Relat Subj Biochem. 1960;22:45–97. doi: 10.1002/9780470122679.ch2. [DOI] [PubMed] [Google Scholar]
LIPMANN F., TUTTLE L. C. Lipase-catalysed condensation of fatty acids with hydroxylamine. Biochim Biophys Acta. 1950 Jan;4(1-3):301–309. doi: 10.1016/0006-3002(50)90036-9. [DOI] [PubMed] [Google Scholar]
LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
MILSTEIN C., SANGER F. An amino acid sequence in the active centre of phosphoglucomutase. Biochem J. 1961 Jun;79:456–469. doi: 10.1042/bj0790456. [DOI] [PMC free article] [PubMed] [Google Scholar]
NATHANS D., LIPMANN F. Amino acid transfer from aminoacyl-ribonucleic acids to protein on ribosomes of Escherichia coli. Proc Natl Acad Sci U S A. 1961 Apr 15;47:497–504. doi: 10.1073/pnas.47.4.497. [DOI] [PMC free article] [PubMed] [Google Scholar]
PORTER G. R., RYDON H. N., SCHOFIELD J. A. Nature of the reactive serine residue in enzymes inhibited by organo-phosphorus compounds. Nature. 1958 Oct 4;182(4640):927–927. doi: 10.1038/182927a0. [DOI] [PubMed] [Google Scholar]
RABINOWITZ M., LIPMANN F. Reversible phosphate transfer between yolk phosphoprotein and adenosine triphosphate. J Biol Chem. 1960 Apr;235:1043–1050. [PubMed] [Google Scholar]
WILLIAMS J., SANGER F. The grouping of serine phosphate residues in phosvitin and casein. Biochim Biophys Acta. 1959 May;33(1):294–296. doi: 10.1016/0006-3002(59)90545-1. [DOI] [PubMed] [Google Scholar]

ACTIONS

RESOURCES