Abstract
Cell fusion between opposite mating types 5 and 21 of the yeast Hansenula wingei is initiated by a strong sexual agglutination reaction. The mating factors responsible for the specificity of cellular recognition are complementary glycoproteins which form a physical complex in vitro . The complex is assayed by recovery of agglutination activity of the multivalent 5-factor after the univalent 21-factor has been inactivated by treatment of the complex with alkali. The 5-factor·21-factor complex, purified on Sepharose 6B, is large (several million daltons) and heterogeneous. The three peaks of 5-factor activity contain a number of combining sites proportional to molecular size.
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 2:46 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 10:22 a.m.) |
Indexed | 1 year, 9 months ago (Nov. 12, 2023, 4:15 a.m.) |
Issued | 51 years, 8 months ago (Jan. 1, 1974) |
Published | 51 years, 8 months ago (Jan. 1, 1974) |
Published Online | 51 years, 8 months ago (Jan. 1, 1974) |
Published Print | 51 years, 8 months ago (Jan. 1, 1974) |
@article{Crandall_1974, title={Molecular Complementarity of Yeast Glycoprotein Mating Factors}, volume={71}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.71.1.26}, DOI={10.1073/pnas.71.1.26}, number={1}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Crandall, Marjorie and Lawrence, Lawrence M. and Saunders, Robert M.}, year={1974}, month=jan, pages={26–29} }