Circular dichroism of pig and bovine lactadherins and their affinity for the pig zona pellucida.
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.
Zayas-Pérez
Héctor
H
Area de Biofisicoquímica, Departamento de Química. Universidad Autónoma Metropolitana-Iztapalapa, Av. San Rafael Atlixco 186, Iztapalapa, C.P. 09340, México, D.F.
Tello-Solís
Salvador R
SR
González-Márquez
Humberto
H
Bonilla-González
Edmundo
E
Mendoza-Hernández
Guillermo
G
Betancourt-Rule
Miguel
M
D000818:Animals; D000954:Antigens, Surface / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002241:Carbohydrates / Q000737:chemistry; D002417:Cattle; D002942:Circular Dichroism; D008892:Milk / Q000737:chemistry; D008894:Milk Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017433:Protein Structure, Secondary; D017422:Sequence Analysis, DNA; D013552:Swine; D015044:Zona Pellucida / Q000378:metabolism*
D000954:Antigens, Surface; D002241:Carbohydrates; D008894:Milk Proteins