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Title: Ultraviolet-induced photodegradation of cucumber (Cucumis sativus L. ) microsomal and soluble protein tryptophanyl residues in vitro

Journal Article · · Plant Physiology; (United States)
OSTI ID:6384009
 [1]
  1. Dept. of Agriculture, Beltsville, MD (United States)

The in vitro effects of ultraviolet B (280--320 nm) radiation on microsomal membrane proteins and partially purified ribulose bisphosphate carboxylase (Rubisco) from cucumber (Cucumis sativus L.) was investigated by measuring the direct photolytic reduction of tryptophan fluorescence and the formation of fluorescent photooxidation products. Exposure of microsomes and Rubisco to monochromatic 300-nm radiation resulted in the loss of intrinsic tryptophan fluorescence and the production of blue-emitting fluorophores. The major product of tryptophan photolysis was tentatively identified as N-formylkynurenine (N-FK). Even though the rates of tryptophan photodegradation and N-FK formation were similar, the amount of blue fluorescence produced was significantly higher in the microsomes relative to Rubisco. Studies with various free radical scavengers and other modifiers indicated that tryptophan photodegradation requires oxygen species. The optimum wavelengths for loss of tryptophan fluorescence were 290 nm for the microsomes and 280 nm for Rubisco. The temperature dependence of tryptophan fluorescence and rate of tryptophan photodegradation indicated an alteration in the cucumber microsomal membranes at about 24[degrees]C, which influenced protein structure and tryptophan photosensitivity. 29 refs., 6 figs., 1 tab.

OSTI ID:
6384009
Journal Information:
Plant Physiology; (United States), Vol. 101:3; ISSN 0032-0889
Country of Publication:
United States
Language:
English