8 rezultatus
The complete sequence of a gamma 3 heavy-chain disease (HCD) protein Wis is presented. The molecule is a dimer of a 289-residue chain linked by 12 disulfide bonds. Protein Wis has an unusual amino terminus, followed by a deletion of most of the VH domain. After a small stretch homologous to the VC
A 20-yr-old black male was admitted with a 5-month history of profound weight loss and diarrhea. Appetite and dietary intake had been remarkably well preserved up until the week before admission. The severity of his depletion was evidenced by a body weight of only 38% of standard, multiple
This paper describes the clinical history of a patient (F.-O.) with longstanding rheumatoid arthritis (RA), who subsequently developed a transient gamma 2-heavy chain disease (gamma 2-HCD). Immunochemical studies comprised serial determinations of serum levels of intact IgG, the gamma-HCD protein,
An abnormal protein, from a petient with mu-chain disease has been studied: protein BUR. It is devoid of the F (ab'')2 mu fragment; molecular weight determinations and immunological data identify the protein as a F(c) 5 mu fragment. Similarly, carbohydrate determinations and proteolysis experiments
The carbohydrate structure and complete amino acid sequence of a human lambda-type immunoglobulin light chain, protein Sm lambda has been determined. The protein was isolated from the urine of a patient with a plasma cell dyscrasia resembling gamma-heavy-chain disease. 13 tryptic peptides covering
A gamma1 protein, designated CRA, found in heavy chain disease contains three inter-heavy disulfide bridges instead of the two normally found in gamma1 immunoglobulin heavy chains. Almost the entire Fd fragment is missing. The NH(2) terminal region is heterogeneous and contains carbohydrate; after
We have studied the structure of a crystallizable gamma 1 heavy-chain disease protein that lacks the entire VH and C gamma 1 domains. The protein starts within the hinge region at aspartic acid 221 (Eu numbering). The native protein is a disulphide-linked dimer with an apparent molecular weight of
Studies of a number of properties of the pathological gammaA-proteins in the first four cases of the recently recognized alpha-chain disease demonstrate that, as in gamma-heavy-chain disease, the abnormal protein is devoid of light chains and represents a portion of the alpha-heavy chain related to