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Solubilization and preliminary characterization of the human ileal vitamin B12-intrinsic factor receptor.
Scand J Clin Lab Invest. 1979 Sep; 39(5):461-7.SJ

Abstract

The human ileal intrinsic factor receptor was solubilized with Triton X-100 using an improved method originally devised for the porcine receptor. At pH 7.4 and in the presence of Ca2+ the receptor bound the vitamin B12 complexes of normal human and pig intrinsic factor but not that of an abnormal biologically inert human intrinsic factor. EGTA dissociated vitamin B12-intrinsic factor from the receptor complexes. The solubilized vitamin B12-intrinsic factor receptor complex consisted of three to four molecular species termed HC-L, HC-20 S, HC-12 S and HC-8.5 S (the three last-mentioned referring to sedimentation coefficients). Of these HC-20 S was the dominating component and had a Stokes radius of 18 nm. Radioactive calcium was shown to be bound to vitamin B12-intrinsic factor and to be contained in its complex with the receptor.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

118515

Citation

Yki-Järvinen, H, et al. "Solubilization and Preliminary Characterization of the Human Ileal Vitamin B12-intrinsic Factor Receptor." Scandinavian Journal of Clinical and Laboratory Investigation, vol. 39, no. 5, 1979, pp. 461-7.
Yki-Järvinen H, Kouvonen I, Gräsbeck R. Solubilization and preliminary characterization of the human ileal vitamin B12-intrinsic factor receptor. Scand J Clin Lab Invest. 1979;39(5):461-7.
Yki-Järvinen, H., Kouvonen, I., & Gräsbeck, R. (1979). Solubilization and preliminary characterization of the human ileal vitamin B12-intrinsic factor receptor. Scandinavian Journal of Clinical and Laboratory Investigation, 39(5), 461-7.
Yki-Järvinen H, Kouvonen I, Gräsbeck R. Solubilization and Preliminary Characterization of the Human Ileal Vitamin B12-intrinsic Factor Receptor. Scand J Clin Lab Invest. 1979;39(5):461-7. PubMed PMID: 118515.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Solubilization and preliminary characterization of the human ileal vitamin B12-intrinsic factor receptor. AU - Yki-Järvinen,H, AU - Kouvonen,I, AU - Gräsbeck,R, PY - 1979/9/1/pubmed PY - 1979/9/1/medline PY - 1979/9/1/entrez SP - 461 EP - 7 JF - Scandinavian journal of clinical and laboratory investigation JO - Scand J Clin Lab Invest VL - 39 IS - 5 N2 - The human ileal intrinsic factor receptor was solubilized with Triton X-100 using an improved method originally devised for the porcine receptor. At pH 7.4 and in the presence of Ca2+ the receptor bound the vitamin B12 complexes of normal human and pig intrinsic factor but not that of an abnormal biologically inert human intrinsic factor. EGTA dissociated vitamin B12-intrinsic factor from the receptor complexes. The solubilized vitamin B12-intrinsic factor receptor complex consisted of three to four molecular species termed HC-L, HC-20 S, HC-12 S and HC-8.5 S (the three last-mentioned referring to sedimentation coefficients). Of these HC-20 S was the dominating component and had a Stokes radius of 18 nm. Radioactive calcium was shown to be bound to vitamin B12-intrinsic factor and to be contained in its complex with the receptor. SN - 0036-5513 UR - https://www.unboundmedicine.com/medline/citation/118515/Solubilization_and_preliminary_characterization_of_the_human_ileal_vitamin_B12_intrinsic_factor_receptor_ L2 - https://www.tandfonline.com/doi/full/10.3109/00365517909106132 DB - PRIME DP - Unbound Medicine ER -