Isolation and purification of cat albumin from cat serum by copper ion affinity chromatography: further analysis of its primary structure.
Proteins, regardless of their origin, have to be highly purified, particularly from the immunochemical point of view, if they are to be used to study their allergenicity. It is shown that cat albumin, a highly potent allergen for cat-sensitive humans, can be isolated and purified from cat serum using immobilized metal ion affinity chromatography (copper ions) instead of a salting-out process or precipitation with alcohol, techniques generally used for the preparation of serum proteins. During the process described, immunoglobulins are concomitantly isolated in a relatively pure form. Cat albumin amino acid composition and sequence were analysed after an ultimate purification by ion-exchange chromatography. The highest homology (greater than 80%) was found with the rat serum albumin.
Dandeu
J P
JP
Unité d'Immuno-Allergie, Institut Pasteur, Paris, France.
Rabillon
J
J
Guillaume
J L
JL
Camoin
L
L
Lux
M
M
David
B
B
D000418:Albumins / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002415:Cats; D002846:Chromatography, Affinity / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods; D003300:Copper; D004591:Electrophoresis, Polyacrylamide Gel; D007074:Immunoglobulin G / Q000276:immunology; D007150:Immunohistochemistry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D012689:Sequence Homology, Nucleic Acid
D000418:Albumins; D000596:Amino Acids; D007074:Immunoglobulin G; D003300:Copper