Insolubilization of L-asparaginase by covalent attachment to nylon tubing

James P. Allison; Lois Davidson; Arthur Gutierrez-Hartman; G. Barrie Kitto

doi:10.1016/S0006-291X(72)80011-1

Insolubilization of L-asparaginase by covalent attachment to nylon tubing

James P. Allison, Lois Davidson, Arthur Gutierrez-Hartman, G. Barrie Kitto

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

Abstract

L-asparaginase has been insolubilized by covalent attachment to partially hydrolyzed nylon tubing via the bifunctional reagent glutar-aldehyde. The Km of the insolubilized enzyme decreases from 3 mM to 0.67 mM L-asparagine with increasing flow rate. The pH optimum of the enzyme is unchanged, although the range of optimal activity is somewhat restricted by insolubilization. Thermal stability of the enzyme is greatly enhanced by insolubilization. The asparaginase-nylon tubing is effective in clearing L-asparagine from human blood and use of the derivative in the asparaginase therapy of acute lymphocytic leukemia is suggested.

Original language	English (US)
Pages (from-to)	66-73
Number of pages	8
Journal	Biochemical and biophysical research communications
Volume	47
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(72)80011-1
State	Published - Apr 14 1972
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(72)80011-1

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title = "Insolubilization of L-asparaginase by covalent attachment to nylon tubing",

abstract = "L-asparaginase has been insolubilized by covalent attachment to partially hydrolyzed nylon tubing via the bifunctional reagent glutar-aldehyde. The Km of the insolubilized enzyme decreases from 3 mM to 0.67 mM L-asparagine with increasing flow rate. The pH optimum of the enzyme is unchanged, although the range of optimal activity is somewhat restricted by insolubilization. Thermal stability of the enzyme is greatly enhanced by insolubilization. The asparaginase-nylon tubing is effective in clearing L-asparagine from human blood and use of the derivative in the asparaginase therapy of acute lymphocytic leukemia is suggested.",

author = "Allison, {James P.} and Lois Davidson and Arthur Gutierrez-Hartman and {Barrie Kitto}, G.",

note = "Funding Information: 1 This research was supported by American Cancer Society Grant T-555.",

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AU - Davidson, Lois

AU - Gutierrez-Hartman, Arthur

AU - Barrie Kitto, G.

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N2 - L-asparaginase has been insolubilized by covalent attachment to partially hydrolyzed nylon tubing via the bifunctional reagent glutar-aldehyde. The Km of the insolubilized enzyme decreases from 3 mM to 0.67 mM L-asparagine with increasing flow rate. The pH optimum of the enzyme is unchanged, although the range of optimal activity is somewhat restricted by insolubilization. Thermal stability of the enzyme is greatly enhanced by insolubilization. The asparaginase-nylon tubing is effective in clearing L-asparagine from human blood and use of the derivative in the asparaginase therapy of acute lymphocytic leukemia is suggested.

AB - L-asparaginase has been insolubilized by covalent attachment to partially hydrolyzed nylon tubing via the bifunctional reagent glutar-aldehyde. The Km of the insolubilized enzyme decreases from 3 mM to 0.67 mM L-asparagine with increasing flow rate. The pH optimum of the enzyme is unchanged, although the range of optimal activity is somewhat restricted by insolubilization. Thermal stability of the enzyme is greatly enhanced by insolubilization. The asparaginase-nylon tubing is effective in clearing L-asparagine from human blood and use of the derivative in the asparaginase therapy of acute lymphocytic leukemia is suggested.

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Insolubilization of L-asparaginase by covalent attachment to nylon tubing

Abstract

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