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Solubilization of the pig ileal intrinsic factor receptor with papain treatment and studies on the solubilized receptor.
Biochim Biophys Acta. 1980 Nov 20; 626(1):244-53.BB

Abstract

The intrinsic factor receptor, known to consist of two subunits alpha and beta, has been solubilized by papain digestion from porcine small intestine. Papain liberates a part of the outermost subunit (alpha) of the receptor. The solubilized part was called papain-alpha. It was purified by affinity chromatography on Sepharose-vitamin B-12-intrinsic factor gel and its molecular dimensions were measured. Its molecular weight measured with SDS-polyacrylamide gel electrophoresis is 45000, its isoelectric point is 4.2 and it binds the cobalamin-intrinsic factor complex in the same way as the whole receptor.

Authors

No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

6257305

Citation

Kouvonen, I. "Solubilization of the Pig Ileal Intrinsic Factor Receptor With Papain Treatment and Studies On the Solubilized Receptor." Biochimica Et Biophysica Acta, vol. 626, no. 1, 1980, pp. 244-53.
Kouvonen I. Solubilization of the pig ileal intrinsic factor receptor with papain treatment and studies on the solubilized receptor. Biochim Biophys Acta. 1980;626(1):244-53.
Kouvonen, I. (1980). Solubilization of the pig ileal intrinsic factor receptor with papain treatment and studies on the solubilized receptor. Biochimica Et Biophysica Acta, 626(1), 244-53.
Kouvonen I. Solubilization of the Pig Ileal Intrinsic Factor Receptor With Papain Treatment and Studies On the Solubilized Receptor. Biochim Biophys Acta. 1980 Nov 20;626(1):244-53. PubMed PMID: 6257305.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Solubilization of the pig ileal intrinsic factor receptor with papain treatment and studies on the solubilized receptor. A1 - Kouvonen,I, PY - 1980/11/20/pubmed PY - 1980/11/20/medline PY - 1980/11/20/entrez SP - 244 EP - 53 JF - Biochimica et biophysica acta JO - Biochim Biophys Acta VL - 626 IS - 1 N2 - The intrinsic factor receptor, known to consist of two subunits alpha and beta, has been solubilized by papain digestion from porcine small intestine. Papain liberates a part of the outermost subunit (alpha) of the receptor. The solubilized part was called papain-alpha. It was purified by affinity chromatography on Sepharose-vitamin B-12-intrinsic factor gel and its molecular dimensions were measured. Its molecular weight measured with SDS-polyacrylamide gel electrophoresis is 45000, its isoelectric point is 4.2 and it binds the cobalamin-intrinsic factor complex in the same way as the whole receptor. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/6257305/Solubilization_of_the_pig_ileal_intrinsic_factor_receptor_with_papain_treatment_and_studies_on_the_solubilized_receptor_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0005-2795(80)90215-9 DB - PRIME DP - Unbound Medicine ER -