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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1967 Aug;58(2):628–634. doi: 10.1073/pnas.58.2.628

The subunit structure and carboxy-terminal sequence of rabbit muscle aldolase.

D E Morse, W Chan, B L Horecker
PMCID: PMC335681  PMID: 5233463

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Selected References

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

  1. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  2. Castellino F. J., Barker R. The binding-sites of rabbit muscle aldolase. Biochem Biophys Res Commun. 1966 Apr 19;23(2):182–187. doi: 10.1016/0006-291x(66)90525-0. [DOI] [PubMed] [Google Scholar]
  3. Chan W., Morse D. E., Horecker B. L. Nonidentity of subunits of rabbit muscle aldolase. Proc Natl Acad Sci U S A. 1967 Apr;57(4):1013–1020. doi: 10.1073/pnas.57.4.1013. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DRECHSLER E. R., BOYER P. D., KOWALSKY A. G. The catalytic activity of carboxypeptidase-degraded aldolase. J Biol Chem. 1959 Oct;234:2627–2634. [PubMed] [Google Scholar]
  5. Ginsburg A., Mehler A. H. Specific anion binding to fructose diphosphate aldolase from rabbit muscle. Biochemistry. 1966 Aug;5(8):2623–2634. doi: 10.1021/bi00872a021. [DOI] [PubMed] [Google Scholar]
  6. HALSEY Y. D., NEURATH H. The terminal carboxyl groups of denatured yeast triosephosphate dehydrogenase. J Biol Chem. 1955 Nov;217(1):247–252. [PubMed] [Google Scholar]
  7. KOWALSKY A., BOYER P. D. A carboxypeptidase-O18-labeled water procedure for determination of CO OH-terminal residues and its application to aldolase. J Biol Chem. 1960 Mar;235:604–608. [PubMed] [Google Scholar]
  8. Kawahara K., Tanford C. The number of polypeptide chains in rabbit muscle aldolase. Biochemistry. 1966 May;5(5):1578–1584. doi: 10.1021/bi00869a018. [DOI] [PubMed] [Google Scholar]
  9. Kobashi K., Lai C. Y., Horecker B. L. Organic phosphate groups in native and borohydride-reduced aldolase. Arch Biochem Biophys. 1966 Nov;117(2):437–444. doi: 10.1016/0003-9861(66)90433-4. [DOI] [PubMed] [Google Scholar]
  10. Penhoet E., Rajkumar T., Rutter W. J. Multiple forms of fructose diphosphate aldolase in mammalian tissues. Proc Natl Acad Sci U S A. 1966 Oct;56(4):1275–1282. doi: 10.1073/pnas.56.4.1275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. ROSE I. A., O'CONNELL E. L., MEHLER A. H. MECHANISM OF THE ALDOLASE REACTION. J Biol Chem. 1965 Apr;240:1758–1765. [PubMed] [Google Scholar]
  12. RUTTER W. J., RICHARDS O. C., WOODFIN B. M. Comparative studies of liver and muscle aldolase. I. Effect of carboxypeptidase on catalytic activity. J Biol Chem. 1961 Dec;236:3193–3197. [PubMed] [Google Scholar]
  13. WINSTEAD J. A., WOLD F. STUDIES ON THE CARBOXYL- AND AMINO-TERMINAL RESIDUES OF RABBIT MUSCLE ALDOLASE. J Biol Chem. 1964 Dec;239:4212–4216. [PubMed] [Google Scholar]
  14. WU C. Y., SHI W. Q. ON THE ROLE OF THE C-TERMINAL TYROSINE RESIDUES OF ALDOLASE. Sci Sin. 1964 Mar;13:459–462. [PubMed] [Google Scholar]
  15. de Vijlder J. J., Slater E. C. The reaction of glyceraldehydephosphate dehydrogenase with NAD+. Biochim Biophys Acta. 1967 Jan 11;132(1):207–209. doi: 10.1016/0005-2744(67)90213-6. [DOI] [PubMed] [Google Scholar]

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