ISSN:
1365-3083
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
The distribution of free and HLA-associated human β2-microglobulin (β2m)in serum, urine, spinal fluid, parotid duct saliva, seminal fluid, amniotic fluid and whey and in membranes from thrombocytes, lymphocytes, neutrophils and fat globules from milk was studied by crossed radioimmunoelectrophoresis (CRIE). The hydrophobic domain of HLA was demonstrable in ‘charge-shift CRIE’ and by binding to phenyl-Sepharose in ‘hydrophobic-interaction CRIE’. In ‘lectin-affinity CRIE’ with concanavalin A and Lens culinaris lectin Sepharose the carbohydrate moiety present in HLA exhibited heterogeneity as judged by the appearance of two partly separated protein peaks. Except for isolated fat globule membranes, HLA-associated β2m was present on all cells investigated. ‘Free’β2m did not contain a hydrophobic domain as assessed by charge-shirt and hydrophobic-interaction CRIE. All body fluids contained β2m in its ‘free’ form only. In serum, besides the free β2m, 2% was present is HLA-associated β2m, which, however, did not contain a hydrophobic domain. A degradation product of ‘free’β2m, with α-mobility, was observed in sera from patients with malignant disorders, rheumatoid arthritis or systemic lupus erythematosus.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-3083.1980.tb00243.x
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