| Autor: |
Lapuk VA; N.D. Zelinsky Institute of Organic Chemistry, USSR Academy of Sciences, Moscow., Tchukhrova AI, Katiashvili NM, Shmakova FV, Kaverzneva ED, Timofeev VP |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 1990 Dec; Vol. 8 (3), pp. 709-20. |
| DOI: |
10.1080/07391102.1990.10507837 |
| Abstrakt: |
Demonstrated herein is the possibility of using the accessibility of tryptophan (Trp) residues in immunoglobulin M (IgM) upon modification with Koshland reagent (2-hydroxy-5-nitrobenzyl bromide) as an index of the conformational changeability of IgM. Of fourteen Trp's in the native IgM (per HL-region) only one appeared to be most accessible, evidently Trp312 in the mu-chain. Irreversible acidic and thermal conformational transitions in IgM increase the number of accessible Trp's approximately two-fold. Following partial enzymatic deglycosylation of IgM, deep scission of mannose in particular, all Trp's become inaccessible. Modification of the most accessible Trp increases 2-3 fold the number of tyrosine residues readily accessible upon nitration with tetranitromethane. Modification of four trp's using spin-label method data causes a sharp reduction of the mobility of the C mu 3 domain and a simultaneous decrease in the solubility of modified IgM. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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