Isolation and characterization of a low-molecular-weight immunoglobulin-binding protein from Yersinia pseudotuberculosis.
A low-molecular-weight immunoglobulin-binding protein (IBP) bound with the cell envelope has been isolated from Yersinia pseudotuberculosis cells and partially characterized. This IBP is a hydrophilic protein with a high polarity index of 55.3%. The molecular weight of the protein has been determined by MALDI-TOF mass spectrometry as 14.3 kD. CD spectroscopy showed that the IBP has high contents of the beta-structure and random coil structure. The IBP contains glycine as the N-terminal amino acid. The protein can be stored for a long time at acidic pH values but aggregates and loses activity at alkaline and neutral pH. The IBP binds rabbit IgG with optimum at pH of 6.0-7.5. The IBP interacts with IgG molecule in the Fc-fragment region. The protein retains activity after heating at 100 degrees C in the presence of SDS.
Sidorin
E V
EV
Pacific Institute of Bioorganic Chemistry, Far-Eastern Division, Russian Academy of Sciences, 690022 Vladivostok, Russia. sev1972@mail.ru.
Kim
N Yu
NY
Leichenko
E V
EV
Anastyuk
S D
SD
Dmitrenok
P S
PS
Naberezhnykh
G A
GA
Solov'eva
T F
TF
D000818:Animals; D002942:Circular Dichroism; D007074:Immunoglobulin G / Q000378:metabolism; D008222:Lymphokines / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D011817:Rabbits; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D015011:Yersinia pseudotuberculosis / Q000737:chemistry*
D007074:Immunoglobulin G; D008222:Lymphokines; C013059:immunoglobulin-binding factors