Cross-linked polypeptide fragments of .beta.-galactosidase

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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435188, 435 76, 530300, 5303871, 530402, G01N 148, C12N 996, C12N 938, A61K 3800

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active

059768576

ABSTRACT:
Formation of an intramolecular cross-link in enzyme donor polypeptide fragments of .beta.-galactosidase, thereby forming a cyclic enzyme donor which is hindered from complementation with an enzyme acceptor fragment to form active of .beta.-galactosidase. The cyclic enzyme donor can be linearized by cleaving to restore complementation ability. Assays in which such cyclic enzyme donors are linearized by specific analytes are disclosed, as well as novel homobifunctional bis-maleimido cross-linking agents of the formula ##STR1## wherein R is hydroxy or acetate.

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Dissertation by Karsten Machholz, University of Gottingen, copyright by Cuvillier Verlag in 1995, accompanied by English translation of excerpts of the dissertation, prepared by Boehringer Mannheim Corporation, Indianapolis.

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