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Vol. 16—1962 - NorthEastern Weed Science Society

Vol. 16—1962 - NorthEastern Weed Science Society

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'. '.32<br />

. dialysis against 'both EDTAand vater. Therefore, ,'wnatever is 'be1ngCh~Fed<br />

,_"is a macromolecule. The precip;ttate itself is 11Iorethan 90%protein but<br />

'does contain SOiftenucleic acid)~ ,sbinepetrtin' tyjle subs.tances and airlaU qUtq1­<br />

'tities of lipid. While we have found that' the .~&fi"tilm of cOmmercial ~~'to%'Us<br />

pectin will, in fact, alter the heat coaSU1abU1~"of pea proteins, tho;<br />

.quanti ties which we have hatt to add to produce this >I'lffeot are so large as<br />

.to be physio16g1cally unimportant in our, e:xperimen~~ ,The. crucial'test, .<br />

of the hypothesis that: pectins 8rtil altering the h~~~ coagulability of ,', .<br />

.proteins would be to isolate the pectins from pee.s~ add them to the proteins<br />

-and exaininethe effect 9fphy'aiological quantitie'is~fth\>se matwrials 01,1 "<br />

the 'heat coagulabilitY' patterns. We are currentl;r. pvrforming such exPeriment.s,<br />

.. . ! .<br />

Wehave also found that the auxin-induced reaction can be inhiBited<br />

,very markedly bY'ethionine at about 10-.3 M.Ano~Elr !ntp.bitor which SQElzaS<br />

to work fairly well is p-fluorOphenye.lanine.Siijde'bcith these substanclilS'<br />

are amino acid antagonists (for tyrosine and methionine rospectively)' We '.<br />

,.,.infer thllt protein synthesis '~ be involved 1ntJ11s auxin-induced roa~ori.<br />

This is a h!ghl$ tentative conclusion which must. ~·'axami.ned further, :.<br />

especially in view of the factthe.t ethionine is aleo'a competitor with .<br />

methionine for methyl group transfer reactions WhiChmayinvolve the pectins.<br />

Other' genara~inhibitors which have been found ett.octiive aro 2-4-dinit1'qphonol,<br />

at about l~ molar, iodoacetic acid at about 10-4 1I!0.larand potassiQlllC1!lnide<br />

at about 10-3 molar. The reactionalilo fails to occur in an atmosphere' :<br />

devoid of oxygen."<br />

Wehave als~ attompted to obtain evidence for .or against the fo;rmation.<br />

of a of anew pr?tein under tha:1pfluonqaof auxin \:)ysubjecting the par,tia1ly<br />

purifiGd soluble supernatant protein to ,electp:ph~sis both on paper and<br />

on starch. Our resUlts to date show that apprClXi!1l8telyfour maj"or peaks.<br />

are present in the electrophoretic patterns ot the: prqtei,tls, at pH 8.6 .. '<br />

with verona'l, ·buffer. .These se6ll1to be. altered qu~ti~atively as a res)1lt<br />

of auxin application, and one new small peak arises as the resUlt of8UXin<br />

application. The interpretation Qt:these :r:esu.J.ts1s ~ome'Hh£'.tuncertain, .<br />

and must nwai-tf'urther work•. Ou,r ,.tentati've concl~on is, however, that ,<br />

auxin treatmont has somehowalterod the protein :spe'ctrum of the cell, ,OM<br />

that such alteration may lead to somo or all ot thegt'owth effects noted'<br />

as a r"sul t of auxin applicotion. . :' . . .<br />

References<br />

A) Some of the data for the conclusions cited above aro"£ound in:<br />

1) Galston. A.W, and Kaur, R. An effect of a\ixins on th0 heat<br />

coagulability of the proteins of growing plant cells. Proc.<br />

Natl. Acad. Sci, (U.S.). l!2,,1587-1590, 195~. '<br />

2) and • The intracollular locale of auxin actiam'<br />

Ane1'l'ect of auxin onthe physical state.~f cytopltsmic proteins.<br />

in. Plant Growth Regulation, Proceedihgs of: the IVth Inti.· Conf'er-J<br />

enoa. 355-362. Iowa State College Press, 'Ames, Iowa. 1961.

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