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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 Jan;71(1):26–29. doi: 10.1073/pnas.71.1.26

Molecular Complementarity of Yeast Glycoprotein Mating Factors

Marjorie Crandall 1,*, Lawrence M Lawrence 1, Robert M Saunders 1
PMCID: PMC387924  PMID: 4521055

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.

Keywords: Hansenula wingei, cellular recognition, Sepharose gel filtration, complementary glycoprotein complex formation

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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