Purification and properties of trehalase(s) from Neurospora

Hill, E. P.; Sussman, Alfred S.

1963-09

Citation: Hill, E. P., Sussman, A. S. (1963/09)."Purification and properties of trehalase(s) from Neurospora." Archives of Biochemistry and Biophysics 102(3): 389-396. <http://hdl.handle.net/2027.42/32198>

Abstract: Trehalase has been obtained in crystalline form from the mycelium of Neurospora crassa. During elution from the first pass through a DEAE-cellulose column, two peaks with trehalase activity were obtained. When the first of these was rechromatographed on DEAE-cellulose, two more major peaks were found. The enzymes of these fractions were compared and found to be similar in substrate specificity, response to inhibitors, pH optima, and Michaelis constants. However, small differences in the rate of inactivation of these enzymes at 50 [deg] were detected.

DOIs: http://dx.doi.org/10.1016/0003-9861(63)90246-7

PMID: 14072517

URI: http://www.sciencedirect.com/science/article/B6WB5-4DW39N7-F2/2/1717884d028aeef62556b00400d96851
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14072517&dopt=citation

Handle: http://hdl.handle.net/2027.42/32198

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