Massachusetts Institute of Technology

University of Iowa Research Foundation

Daniel L Lohse

Robert Samuel Langer

Robert J Linhardt

Charles L Cooney

Ramnath Sasisekharan

A single, reproducible scheme to simultaneously purify all three of the heparin lyases from F. heparinum to apparent homogeneity is disclosed herein. The kinetic properties of the heparin lyases have been determined as well as the conditions to optimize their activity and stability. Mono-clonal antibodies to the three heparinases are also described and are useful for detection, isolation and characterization of the heparinases.

Purification, composition and specificity of Heparinase I, II, and III from Flavobacterium heparinum

A purified heparinase I, II and III free of lyase activity and each having a molecular weight of 42,800 84,100, 70,800, respectively, are produced by culturing Flavobacterium heparinum. The kinetic properties of the heparinases have been determined as well as the conditions to optimize their activity and stability.

Purification of Heparinase I, II and III from Flavobacterium heparinum

A single, reproducible scheme to simultaneously purify all three of the heparin lyases from F. heparinum to apparent homogeneity is disclosed herein. The kinetic properties of the heparin lyases have been determined as well as the conditions to optimize their activity and stability. Monoclonal antibodies to the three heparinases are also described and are useful for detection, isolation and characterization of the heparinases.

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Bryan, TX, United States of America

Daniel L Lohse