Specificity of an immunoaffinity column for odorant-binding protein from bovine nasal mucosa
- 1 December 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Chemical Senses
- Vol. 12 (4) , 601-608
- https://doi.org/10.1093/chemse/12.4.601
Abstract
The odorant-binding protein from bovine nasal mucosa, purified by fast protein liquid chromatography, has been used to elicit polyclonal antibodies in a New Zealand white rabbit and to prepare an affinity Sepharose 4B column. The antibodies have been purified through the affinity column and used to prepare an immunoadsorbent for specific and efficient purification of bovine odorant-binding protein. The immunoadsorbent does not bind proteins of comparable molecular weight, including the olfactory marker protein, which are localized in the primary olfactory pathway. Furthermore, the immunoadsorbent does not bind the odorant-binding protein present in the nasal mucosa of other animal species.This publication has 7 references indexed in Scilit:
- Odorant-binding protein: localization to nasal glands and secretions.Proceedings of the National Academy of Sciences, 1986
- Occurrence of a pyrazine binding protein in the nasal mucosa of some vertebratesComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1986
- Purification and characterisation of an odorant‐binding protein from cow nasal tissueEuropean Journal of Biochemistry, 1985
- Isolation and characterization of an olfactory receptor protein for odorant pyrazines.Proceedings of the National Academy of Sciences, 1985
- Specificity of a pyrazine binding protein from cow olfactory mucosaChemical Senses, 1985
- Amino acid sequence of the precursor of rat liver alpha 2 micro-globulin.Journal of Biological Chemistry, 1981
- Isolation and characterization of rat olfactory marker protein.Journal of Biological Chemistry, 1976