Title : Preparation and initial characterization of an intermediate, half-cleaved form of human alpha 2-macroglobulin.

Pub. Date : 1989 Jun 27

PMID : 2476174






3 Functional Relationships(s)
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1 Comparison of ESR results obtained from spin-labeling methylamine-treated or protease-reacted alpha 2M with those from spin-labeling of the free SH groups in intermediate-form alpha 2M shows that trapped protease influences the mobility of the attached nitroxide either through direct contact or by producing a different conformation from that present in methylamine-treated or intermediate-form alpha 2M. Hydroxylamine alpha-2-macroglobulin Homo sapiens
2 Comparison of ESR results obtained from spin-labeling methylamine-treated or protease-reacted alpha 2M with those from spin-labeling of the free SH groups in intermediate-form alpha 2M shows that trapped protease influences the mobility of the attached nitroxide either through direct contact or by producing a different conformation from that present in methylamine-treated or intermediate-form alpha 2M. Hydroxylamine alpha-2-macroglobulin Homo sapiens
3 Comparison of ESR results obtained from spin-labeling methylamine-treated or protease-reacted alpha 2M with those from spin-labeling of the free SH groups in intermediate-form alpha 2M shows that trapped protease influences the mobility of the attached nitroxide either through direct contact or by producing a different conformation from that present in methylamine-treated or intermediate-form alpha 2M. Hydroxylamine alpha-2-macroglobulin Homo sapiens