Abstract
Commercial preparations of human ceruloplasmin were chromatographed on hydroxyapatite by the gradient elution technique. From two batches originating from different Cohn fractions, five forms of the protein were isolated. One of these appeared upon aging of one of the batches. Chemical analysis showed that the ceruloplasmin forms differed only in their carbohydrate content, with the exception of two of the forms (IIa and IIb) which had identical chemical composition. The total carbohydrate content of the ceruloplasmin forms varied between 6% and 10%. Two of the forms (IIa and IIb) were supposed to represent conformational variants of native ceruloplasmin components. It is concluded that at least three forms of ceruloplasmin are present in human serum. The polymorphism of human ceruloplasmin is discussed in the light of recent examinations of other glycoproteins.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
