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Evaluation of two sources of soluble HL-A antigens: platelets and serum

✍ Scribed by M. A. Pellegrino; S. Ferrone; Anna G. Pellegrino; S. K. Oh; R. A. Reisfeld

Book ID
102821168
Publisher
John Wiley and Sons
Year
1974
Tongue
English
Weight
640 KB
Volume
4
Category
Article
ISSN
0014-2980

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✦ Synopsis

Abstract

Platelets and human serum have been evaluated as sources for extraction of soluble HL‐A antigens. 3 M KCl was found to efficiently solubilize HL‐A antigens from platelets with a recovery ranging between 50 and 100 %. However, because of the low density of HL‐A determinants on platelets, the yield of soluble antigens is low, as only 1 mg of protein can be recovered from 1 Γ— 10^9^ platelets. Thus, while it is difficult to solubilize sufficient antigens from platelets for chemical characterization, it is possible to use these materials for biological applications such as pretreatment of kidney recipients. Soluble HL‐A antigen is present in human serum, since following extensive ultracentrifugation, it can still effectively inhibit the cytotoxic activity of HL‐A alloantisera. The same HL‐A specificities were found to be present in varying amounts among different donors. Partial purification of such antigens can be achieved by ion‐exchange chromatography of serum on QAE‐Sephadex.

πŸ“œ SIMILAR VOLUMES

The preparation and purification of HL-A
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✍ R. Voigtmann; G. Uhlenbruck; G. I. Pardoe; K. Rogers πŸ“‚ Article πŸ“… 1974 πŸ› John Wiley and Sons 🌐 English βš– 577 KB

## Abstract HL‐A‐active protein fragments have been isolated from lymphoid sources (tonsillar tissue, cells from lymphoblastoid cell lines (LCL cells)) and from platelets. The yields and specific activities of products obtained by enzymic chaotropic treatment indicate the superiority of 3 M KCl ext