STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. V. THE OXIDATION BOHR EFFECT IN NORMAL HUMAN HEMOGLOBIN AND HUMAN HEMOGLOBIN DIGESTED WITH CARBOXYPEPTIDASE A - PubMed (original) (raw)
- PMID: 14321368
Free article
STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. V. THE OXIDATION BOHR EFFECT IN NORMAL HUMAN HEMOGLOBIN AND HUMAN HEMOGLOBIN DIGESTED WITH CARBOXYPEPTIDASE A
M BRUNORI et al. J Biol Chem. 1965 Aug.
Free article
No abstract available
Similar articles
- STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. II. CARBOXYPEPTIDASE DIGESTS OF HUMAN HEMOGLOBIN.
BRUNORI M, ANTONINI E, WYMAN J, ZITO R, TAYLOR JF, ROSSI-FANELLI A. BRUNORI M, et al. J Biol Chem. 1964 Jul;239:2340-4. J Biol Chem. 1964. PMID: 14209966 No abstract available. - Effect of heme and non-heme ligands on subunit dissociation of normal and carboxypeptidase-digested hemoglobin. Gel filtration and flash photolysis studies.
Chiancone E, Anderson NM, Antonini E, Bonaventura J, Bonaventura C, Brunori M, Spagnuolo C. Chiancone E, et al. J Biol Chem. 1974 Sep 25;249(18):5689-94. J Biol Chem. 1974. PMID: 4413057 No abstract available. - STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. I. HUMAN HEMOGLOBIN.
ANTONINI E, WYMAN J, BRUNORI M, TAYLOR JF, ROSSI-FANELLI A, CAPUTO A. ANTONINI E, et al. J Biol Chem. 1964 Mar;239:907-12. J Biol Chem. 1964. PMID: 14154472 No abstract available. - Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease States.
Reeder BJ, Wilson MT. Reeder BJ, et al. Curr Med Chem. 2005;12(23):2741-51. doi: 10.2174/092986705774463021. Curr Med Chem. 2005. PMID: 16305469 Review. - How much do we know about the Bohr effect of hemoglobin?
Ho C, Russu IM. Ho C, et al. Biochemistry. 1987 Oct 6;26(20):6299-305. doi: 10.1021/bi00394a001. Biochemistry. 1987. PMID: 3322377 Review. No abstract available.
Cited by
- The interaction of inositol hexaphosphate with methaemoglobin.
Kilmartin JV. Kilmartin JV. Biochem J. 1973 Aug;133(4):725-33. doi: 10.1042/bj1330725. Biochem J. 1973. PMID: 4748831 Free PMC article. - Conformational changes induced by polyanions in haemoglobin from Camelus dromedarius. Studies on the ferric derivatives.
Santucci R, Ascoli F, Amiconi G, Brunori M. Santucci R, et al. Biochem J. 1986 May 1;235(3):791-5. doi: 10.1042/bj2350791. Biochem J. 1986. PMID: 3753446 Free PMC article. - Redox equilibria of liganded forms of methemoglobin.
Bull C, Hoffman BM. Bull C, et al. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3382-6. doi: 10.1073/pnas.72.9.3382. Proc Natl Acad Sci U S A. 1975. PMID: 242002 Free PMC article. - Linearity of the hemoglobin oxidation bohr effect.
Hoffman BM, Bull C. Hoffman BM, et al. Proc Natl Acad Sci U S A. 1976 Mar;73(3):800-3. doi: 10.1073/pnas.73.3.800. Proc Natl Acad Sci U S A. 1976. PMID: 1062790 Free PMC article. - Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control.
Huang Z, Shiva S, Kim-Shapiro DB, Patel RP, Ringwood LA, Irby CE, Huang KT, Ho C, Hogg N, Schechter AN, Gladwin MT. Huang Z, et al. J Clin Invest. 2005 Aug;115(8):2099-107. doi: 10.1172/JCI24650. Epub 2005 Jul 21. J Clin Invest. 2005. PMID: 16041407 Free PMC article.