Direct reciprocal allosteric interaction of oxygen and hydrogen carbonate sequence of the haemoglobins of the Caiman (Caiman crocodylus), the Nile crocodile (Crocodylus niloticus) and the Mississippi crocodile (Alligator mississippiensis)
- PMID: 6286445
Direct reciprocal allosteric interaction of oxygen and hydrogen carbonate sequence of the haemoglobins of the Caiman (Caiman crocodylus), the Nile crocodile (Crocodylus niloticus) and the Mississippi crocodile (Alligator mississippiensis)
Similar articles
-
[Direct allosteric interaction of oxygen and bicarbonate: N-acetyl-alanyl-seryl-phenylalanine, N-terminal sequence of the beta-chains of the haemoglobins of Nil crocodile (Crocodylusniloticus) and Mississippi crocodile (Alligator mississippiensis) (author's transl)].Z Naturforsch C Biosci. 1981 Sep-Oct;36(9-10):902-3. Z Naturforsch C Biosci. 1981. PMID: 7303821 German.
-
Caiman crocodylus hemoglobin. Complete primary structures of alpha and beta chains; phylogenic and regulatory aspects.Int J Pept Protein Res. 1982 Oct;20(4):337-50. Int J Pept Protein Res. 1982. PMID: 7174198
-
Transplanting a unique allosteric effect from crocodile into human haemoglobin.Nature. 1995 Jan 19;373(6511):244-6. doi: 10.1038/373244a0. Nature. 1995. PMID: 7816138
-
Similarity of Crocodilian and Avian Lungs Indicates Unidirectional Flow Is Ancestral for Archosaurs.Integr Comp Biol. 2015 Dec;55(6):962-71. doi: 10.1093/icb/icv078. Epub 2015 Jul 3. Integr Comp Biol. 2015. PMID: 26141868 Review.
-
Tick-crocodilian interactions: a review, with the first record of tick (Acari: Ixodidae) infestation in the saltwater crocodile (Crocodylus porosus), and a concise host-parasite index.Exp Appl Acarol. 2019 May;78(1):127-132. doi: 10.1007/s10493-019-00378-0. Epub 2019 May 15. Exp Appl Acarol. 2019. PMID: 31093858 Review.
Cited by
-
Hemoglobin Long Island is caused by a single mutation (adenine to cytosine) resulting in a failure to cleave amino-terminal methionine.Proc Natl Acad Sci U S A. 1986 Jan;83(1):24-7. doi: 10.1073/pnas.83.1.24. Proc Natl Acad Sci U S A. 1986. PMID: 3455755 Free PMC article.
-
Primary structure of hemoglobin alpha-chain of Columba livia (gray wild pigeon).J Protein Chem. 1989 Oct;8(5):629-46. doi: 10.1007/BF01025603. J Protein Chem. 1989. PMID: 2610857
-
Universal regularities in protein primary structure: preference in bonding and periodicity.Orig Life Evol Biosph. 1986;17(1):35-49. doi: 10.1007/BF01809811. Orig Life Evol Biosph. 1986. PMID: 3796966
-
Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO2.Am J Physiol Regul Integr Comp Physiol. 2020 Mar 1;318(3):R657-R667. doi: 10.1152/ajpregu.00342.2019. Epub 2020 Feb 5. Am J Physiol Regul Integr Comp Physiol. 2020. PMID: 32022587 Free PMC article.
-
The effects of temperature and pH on secondary structure and antioxidant activity of Crocodylus siamensis hemoglobin.Protein J. 2012 Jan;31(1):43-50. doi: 10.1007/s10930-011-9372-7. Protein J. 2012. PMID: 22101803
Publication types
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources