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The hydrophobic nature of the pig intrinsic factor receptor in the intestine.
Biochim Biophys Acta. 1981 Aug 20; 646(2):268-73.BB

Abstract

The pig intestinal intrinsic factors receptor has been isolated and dissociated into its alpha and beta subunits. The beta subunit was found to be more hydrophobic than the alpha subunit. In a detergent solution only the alpha subunit was accessible to digestion with papain. The whole isolated receptor was introduced into artificial single bilayer liposomes where is apparently was randomly oriented. Liposomes containing the receptor were digested with papain and the polypeptide segments that stayed in the lipid fraction were extracted and analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Four species were found with Mr values of 23 000, 45 000, 70 000 and 86 000.

Authors

No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

6271201

Citation

Kouvonen, I. "The Hydrophobic Nature of the Pig Intrinsic Factor Receptor in the Intestine." Biochimica Et Biophysica Acta, vol. 646, no. 2, 1981, pp. 268-73.
Kouvonen I. The hydrophobic nature of the pig intrinsic factor receptor in the intestine. Biochim Biophys Acta. 1981;646(2):268-73.
Kouvonen, I. (1981). The hydrophobic nature of the pig intrinsic factor receptor in the intestine. Biochimica Et Biophysica Acta, 646(2), 268-73.
Kouvonen I. The Hydrophobic Nature of the Pig Intrinsic Factor Receptor in the Intestine. Biochim Biophys Acta. 1981 Aug 20;646(2):268-73. PubMed PMID: 6271201.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The hydrophobic nature of the pig intrinsic factor receptor in the intestine. A1 - Kouvonen,I, PY - 1981/8/20/pubmed PY - 1981/8/20/medline PY - 1981/8/20/entrez SP - 268 EP - 73 JF - Biochimica et biophysica acta JO - Biochim Biophys Acta VL - 646 IS - 2 N2 - The pig intestinal intrinsic factors receptor has been isolated and dissociated into its alpha and beta subunits. The beta subunit was found to be more hydrophobic than the alpha subunit. In a detergent solution only the alpha subunit was accessible to digestion with papain. The whole isolated receptor was introduced into artificial single bilayer liposomes where is apparently was randomly oriented. Liposomes containing the receptor were digested with papain and the polypeptide segments that stayed in the lipid fraction were extracted and analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Four species were found with Mr values of 23 000, 45 000, 70 000 and 86 000. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/6271201/The_hydrophobic_nature_of_the_pig_intrinsic_factor_receptor_in_the_intestine_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0005-2736(81)90333-3 DB - PRIME DP - Unbound Medicine ER -