Title : Identification and properties of J chain isolated from catfish macroglobulin.

Pub. Date : 1975 Oct

PMID : 809510






5 Functional Relationships(s)
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1 After the cleavage of disulfide bonds of macroglobulin isolated from channel catfish (Ictalurus punctatus), an electrophoretically fast-moving polypeptide, which resembled human J chain, was released. Disulfides joining chain of multimeric IgA and IgM Homo sapiens
2 On a Sephadex G-200 column equilibrated in 5 M guanidine, the elution position of the J chain overlapped with the descending part of the L chain peak. sephadex joining chain of multimeric IgA and IgM Homo sapiens
3 On a Sephadex G-200 column equilibrated in 5 M guanidine, the elution position of the J chain overlapped with the descending part of the L chain peak. Guanidine joining chain of multimeric IgA and IgM Homo sapiens
4 A comparison of catfish and human J chain amino acid analyses showed the former to have a higher content of serine, glycine, and phenylalanine and a lower content of aspartic acid, isoleucine, and arginine. Serine joining chain of multimeric IgA and IgM Homo sapiens
5 A comparison of catfish and human J chain amino acid analyses showed the former to have a higher content of serine, glycine, and phenylalanine and a lower content of aspartic acid, isoleucine, and arginine. Phenylalanine joining chain of multimeric IgA and IgM Homo sapiens