Purification of egg yolk immunoglobulins. A two-step procedure using hydrophobic interaction chromatography and gel filtration.
نویسندگان
چکیده
A two-step chromatographic procedure was developed for the isolation and purification of hen IgY antibodies from egg yolk. The antibodies were completely separated from vitellin and lipids by hydrophobic interaction chromatography followed by gel filtration. Almost no residual yolk proteins, no immunoglobulin aggregates, and no antibody fragments could be detected in the final extract. Moreover, the method described, guarantees the recovery of antibodies of undiminished activity. Although the final yield is somewhat lower than that obtained by an isolation method consisting of two precipitation steps with polyethylene glycol and alcohol respectively, the procedure described is particularly recommended when highly purified antibody preparations are needed.
منابع مشابه
Single-step purification of F(ab')2 fragments of mouse monoclonal antibodies (immunoglobulins G1) by hydrophobic interaction high performance liquid chromatography using TSKgel Phenyl-5PW.
Hydrophobic interaction high performance liquid chromatography (HPLC) using TSKgel Phenyl-5PW was applicable to single-step purification of F(ab')2 fragments from pepsin digests of mouse monoclonal antibodies of IgG1 class. The digests were applied to the gel equilibrated with phosphate-buffered saline containing 1 M ammonium sulfate. F(ab')2 fragments were adsorbed onto the gel using the same ...
متن کاملSnake egg immunoglobulins: biochemical characteristics and adjusted isolation procedure.
Transmission of specific immunoglobulins from mothers to their offspring via the egg is a common phenomenon in egg-laying vertebrates but the occurrence of this phenomenon in reptiles, especially in colubrid snakes, has not been proven until recently. Thus, the essential biochemical characteristics of antibodies deposited in eggs of Elaphe guttata (Colubridae, Serpentes) were studied after isol...
متن کاملISOLATION AND PURIFICATION OF RIBOFLAVIN BINDING PROTIEN FROM COOT EGG-YOLK (Fulica atra)
Riboflavin-binding protein (RfBP) was isolated, purified and characterized from Coot (Fulica atra) egg. The RfBP was purified using DEAE-Sepharose ion exchange chromatography followed by gel filtration on Sephadex G-100. The purity of the proteins was judged by SDSPAGE. The protein migrated as a single band on SDS gel with a molecular weight of corresponding to nearly 29 Kd.
متن کاملOn hen egg fractionation: applications of liquid chromatography to the isolation and the purification of hen egg white and egg yolk proteins.
Liquid chromatography has been used as a means of egg protein analysis or as a method for the purification of egg proteins. Several chromatographic methods, including gel permeation, ion-exchange, reversed-phase, hydrophobic interaction, and immobilized-ligand-affinity chromatography, have been carried out for the separation or the purification of egg yolk or egg white proteins. Ion-exchange ch...
متن کاملPurification of immunoglobulins from chicken sera by thiophilic gel chromatography.
Immunoglobulin Y is different from most of the other immunoglobulins because it does not bind protein A or protein G. Thiophilic gel chromatography has been successfully used to purify IgY from chicken egg yolk, but the technology has not previously been used to purify IgY from serum. In this research note, we describe the optimization of T-gel chromatography for purification of IgY from serum....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of immunological methods
دوره 110 2 شماره
صفحات -
تاریخ انتشار 1988