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Plant Physiology 61:501-505 (1978)
© 1978 American Society of Plant Biologists

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Articles

Proteases of Senescing Oat Leaves

II. Reaction to Substrates and Inhibitors 1

Rolf H. Drivdahl2 and Kenneth V. Thimann3

Thimann Laboratories, University of California, Santa Cruz, California 95064

Two proteases isolated from senescent oat (Avena sativa) leaves have been subjected to further study. One of these, an acid protease active at pH 4.2, is inhibited by phenylmethylsulfonyl fluoride (PMSF) but not by iodoacetamide (IAc). The other, active at pH 6.6, is inhibited by both PMSF and IAc. These results, together with previously reported evidence that mercaptoethanol stimulates the activity of only the neutral protease, are taken to indicate that the acid protease is probably of the serine type, whereas the neutral enzyme is of the sulfhydryl type. Both enzymes are inhibited by irradiation in the presence of rose bengal, a selective histidine modification reagent. The acid protease was completely unaffected by chelators, but data on the neutral protease were equivocal.

All protein substrates tested were attacked by both enzymes, though at strikingly different rates. Characterization of the digestion products, with denatured hemoglobin as substrate, indicated that the acidic enzyme is an endoprotease, while the neutral one is an exoprotease. Evidence is presented that these proteases undergo autolysis in vitro.

2 Present address: 1521 Pine Street, Olympia, Washington 98502.

3 To whom requests for reprints should be sent.

1 Supported in part by National Science Foundation Grant GB 35238 to K. V. T.






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Copyright © 1978 by the American Society of Plant Biologists