| Autor: |
Cramer, R., Soranzo, M.R., Patriarca, P. |
| Zdroj: |
Blood; December 1981, Vol. 58 Issue: 6 p1112-1118, 7p |
| Abstrakt: |
Human eosinophils from subjects with or without myeloperoxidase (MPO) deficiency and guinea pig eosinophils are able to decarboxylate l-alanine in the presence of the cationic detergent cetyltrimethylammonium bromide (CTAB) but not in the presence of the nonionic detergent Triton X-100. Instead, both normal human neutrophils and guinea pig neutrophils decarboxylate l-alanine in the presence of either detergent. When the non-bromide-containing cationic detergent cetyltrimethylammonium hydroxide (CTAOH) is used instead of CTAB, the eosinophils from MPO-deficient subjects are unable to decarboxylate l-alanine. Decarboxylation occurs with the combination CTAOH-Br–, but not with the combinations CTAOH-I–, CTAOH-CI–, or CTAOH-F–. Bromide in the absence of CTAOH does not promote decarboxylation. Triton X-100 and deoxycholate are much less effective in promoting decarboxylation in the presence of bromide. l-Lysine and l-aspartic acid are decarboxylated to a considerably lower rate than l-alanine in the presence of CTAOH and Br–. It is concluded that the eosinophils can catalyze the bromide-dependent decarboxylation of the apolar amino acid l-alanine in the presence of a cationic detergent. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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