Postsecretory modifications of streptavidin
- 15 April 1989
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 259 (2), 369-376
- https://doi.org/10.1042/bj2590369
Abstract
Streptavidin, an extracellular biotin-binding protein from Streptomyces avidinii, exhibits a multiplicity in its electrophoretic mobility pattern which depends both upon the conditions for growth of the bacterium and upon the protocol used in the purification of the protein. The observed structural heterogeneity appears to reflect the action of two types of postsecretory molecular events: proteolytic digestion of the intact Mr-18,000 subunit to a minimal molecular size (approx. Mr 14,000), and aggregation of the native tetramer into higher-order oligomeric forms. The extent of subunit degradation and/or tetrameric aggregation affects the capacity of a given streptavidin preparation to interact with biotin-conjugated proteins in different assay systems.This publication has 17 references indexed in Scilit:
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