Circular Dichroism of Pig and Bovine Lactadherins and Their Affinity for the Pig Zona Pellucida

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We have purified and characterized pig and bovine milk lactadherins. Studies by circular dichroism spectroscopy indicate that the two proteins present a similar folding pattern. Results have been discussed in terms of their affinity for pig zona pellucida in order to use these proteins as analogs of pig sperm lactadherin in gamete studies.

Keywords: bovine; chaperone; circular dichroism; dnak; milk lactadherin; pig; zona pellucida

Document Type: Review Article


Affiliations: Area de Biofisicoquimica, Departamento de Quimica. Universidad Autonoma Metropolitana-Iztapalapa, Av. San Rafael Atlixco 186, Iztapalapa, C.P. 09340, Mexico,D.F.

Publication date: April 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.



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