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- BARTLETT G. R. Phosphorus assay in column chromatography. J Biol Chem. 1959 Mar;234(3):466–468. [PubMed] [Google Scholar]
- COLEMAN J. E., VALLEE B. L. Metallocarboxypeptidases. J Biol Chem. 1960 Feb;235:390–395. [PubMed] [Google Scholar]
- COOMBS T. L., OMOTE Y., VALLEE B. L. THE ZINC-BINDING GROUPS OF CARBOXYPEPTIDASE A. Biochemistry. 1964 May;3:653–662. doi: 10.1021/bi00893a010. [DOI] [PubMed] [Google Scholar]
- Cohen S. R., Wilson I. B. Measurement of the zinc dissociation constants of alkaline phosphatase from Escherichia coli by equilibration with zinc ion buffers. Biochemistry. 1966 Mar;5(3):904–909. doi: 10.1021/bi00867a014. [DOI] [PubMed] [Google Scholar]
- Duff T. A., Coleman J. E. Macaca mulata carbonic anhydrase. Crystallization and physicochemical and enzymatic properties of two isozymes. Biochemistry. 1966 Jun;5(6):2009–2019. doi: 10.1021/bi00870a032. [DOI] [PubMed] [Google Scholar]
- HORINISHI H., HACHIMORI Y., KURIHARA K., SHIBATA K. STATES OF AMINO ACID RESIDUES IN PROTEINS. 3. HISTIDINE RESIDUES IN INSULIN, LYSOZYME, ALBUMIN AND PROTEINASES AS DETERMINED WITH A NEW REAGENT OF DIAZO-I-H-TETRAZOLE. Biochim Biophys Acta. 1964 Jun 8;86:477–489. [PubMed] [Google Scholar]
- MALAMY M. H., HORECKER B. L. RELEASE OF ALKALINE PHOSPHATASE FROM CELLS OF ESCHERICHIA COLI UPON LYSOZYME SPHEROPLAST FORMATION. Biochemistry. 1964 Dec;3:1889–1893. doi: 10.1021/bi00900a017. [DOI] [PubMed] [Google Scholar]
- Neu H. C., Heppel L. A. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem. 1965 Sep;240(9):3685–3692. [PubMed] [Google Scholar]
- PLOCKE D. J., LEVINTHAL C., VALLEE B. L. Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme. Biochemistry. 1962 May 25;1:373–378. doi: 10.1021/bi00909a001. [DOI] [PubMed] [Google Scholar]
- PLOCKE D. J., VALLEE B. L. Interaction of alkaline phosphatase of E. coli with metal ions and chelating agents. Biochemistry. 1962 Nov;1:1039–1043. doi: 10.1021/bi00912a014. [DOI] [PubMed] [Google Scholar]
- PLOTCH S., LUKTON A. ACTIVE SITE STUDIES OF BACTERIAL ALKALINE PHOSPHATASE. Biochim Biophys Acta. 1965 Apr 26;99:181–182. doi: 10.1016/s0926-6593(65)80022-4. [DOI] [PubMed] [Google Scholar]
- RIORDAN J. F., VALLEE B. L. ACETYLCARBOXYPEPTIDASE. Biochemistry. 1963 Nov-Dec;2:1460–1468. doi: 10.1021/bi00906a045. [DOI] [PubMed] [Google Scholar]
- ROTHMAN F., BYRNE R. Fingerprint analysis of alkaline phosphatase of Escherichia coli K12. J Mol Biol. 1963 Apr;6:330–340. doi: 10.1016/s0022-2836(63)80092-3. [DOI] [PubMed] [Google Scholar]
- SCHWARTZ J. H., LIPMANN F. Phosphate incorporation into alkaline phosphatase of E. coli. Proc Natl Acad Sci U S A. 1961 Dec 15;47:1996–2005. doi: 10.1073/pnas.47.12.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schlesinger M. J., Barrett K. The reversible dissociation of the alkaline phosphatase of Escherichia coli. I. Formation and reactivation of subunits. J Biol Chem. 1965 Nov;240(11):4284–4292. [PubMed] [Google Scholar]
- VALLEE B. L. ACTIVE CENTER OF CARBOXYPEPTIDASE A. Fed Proc. 1964 Jan-Feb;23:8–17. [PubMed] [Google Scholar]
- VISWANATHA T., LAWSON W. B., WITKOP B. The action of N-bromosuccinimide on trypsinogen and its derivatives. Biochim Biophys Acta. 1960 May 20;40:216–224. doi: 10.1016/0006-3002(60)91345-7. [DOI] [PubMed] [Google Scholar]
- WEIL L., BUCHERT A. R. Photoöxidation of crystalline beta-lactoglobulin in the presence of methylene blue. Arch Biochem Biophys. 1951 Nov;34(1):1–15. doi: 10.1016/s0003-9861(51)80003-1. [DOI] [PubMed] [Google Scholar]
- WILSON I. B., DAYAN J., CYR K. SOME PROPERTIES OF ALKALINE PHOSPHATASE FROM ESCHERICHIA COLI. TRANSPHOSPHORYLATION. J Biol Chem. 1964 Dec;239:4182–4185. [PubMed] [Google Scholar]