A glutaraldehyde (GA) spacer complex on enzyme immobilization was cleaved from the support introduced Nα -9-fluorenylmethyl-oxycarbonylglycine. By the 1H-NMR spectroscopic measurement of the desired complex, glycine-GA-phenethylamine (GGP), GA was thought to be involved in enzyme immobilization as a heteropolymer with the molecular weight range of about 600 to 1300. © 1997, Taylor &
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