Accessibility of Tryptophan Residues in Immunoglobulin M as an Index of Its Conformational Changeability Full article
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Journal of Biomolecular Structure & Dynamics
ISSN: 0739-1102 , E-ISSN: 1538-0254 |
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Output data | Year: 1990, Volume: 8, Number: 3, Pages: 709-720 Pages count : 12 DOI: 10.1080/07391102.1990.10507837 | ||||
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Abstract:
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 μ-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 Cμ3 domain and a simultaneous decrease in the solubility of modified IgM.
Cite:
Lapuk V.A.
, Tchukhrova A.I.
, Katiashvili N.M.
, Shmakova F.V.
, Kaverzneva E.D.
, Timofeev V.P.
Accessibility of Tryptophan Residues in Immunoglobulin M as an Index of Its Conformational Changeability
Journal of Biomolecular Structure & Dynamics. 1990. V.8. N3. P.709-720. DOI: 10.1080/07391102.1990.10507837 OpenAlex
Accessibility of Tryptophan Residues in Immunoglobulin M as an Index of Its Conformational Changeability
Journal of Biomolecular Structure & Dynamics. 1990. V.8. N3. P.709-720. DOI: 10.1080/07391102.1990.10507837 OpenAlex
Identifiers:
OpenAlex: | W2002922084 |
Citing:
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OpenAlex | 3 |