A study of some plant esterases

Schwartz, H. M.; Biedron, Sieglinde I.; Holdt, M. M. von; Rehm, S.

doi:10.1016/s0031-9422(00)88039-5

Cited by 59 publications

(12 citation statements)

References 15 publications

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“…The esterases observed in these experiments may be related to the breakdown of the onion's storage proteins (Mallery 1971). It has been suggested by Schwartz et al •(1964) that carboxylic ester hydrolase activity may be due in part to proteinases or peptidases. This seems unlikely in light of the fact that Fottrell (1968) was unable to detect any activity of root nodule esterases to benzoyl-DL-arginine-|3-naphthylamide, a substrate hydrolyzed by proteolytic enzymes, and that none of the AmP isoenzymes detected in the onion corresponded in REM to any EST fraction.…”

Section: Discussionmentioning

confidence: 61%

Isoenzyme Activities during the Early Stages of Allium Radicle Germination

Mallery

1972

Physiologia Plantarum

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As a continuation of a study of the molecular events surrounding the establisbment of a mature root apex, changes in tbe pattern and specific activity of the isoenzymes of aminopeptidase (AmP), esterase (EST), glueose-6-pbospbate dehydrogenase (G6PD) and glutamic-oxaloacetic transaminase (GOT) were investigated during the early germinative growth of the Allium radicle tip.Polyacrylamide disc gel eleetrophoresis revealed a total of 9 EST fractions. A shift in pattern and reactivity characteristic of pre-emergence to those characteristic of post-emergence was demonstrated.G6PD electropberograms displayed 5 isoenzyme bands. Relative specific activity analyses indicated that this enzyme may be more important during tbe very early stages of germination.Only quantitative differences were noted in tbe 3 AmP isoenzymes detected. The progressive increase in AmP isoenzyme activity during the period of maximal protein body degradation suggested a role for these exopeptidases in tbe degradation of reserve proteins.The 3 isoenzyme bands of GOT exhibited only quantitative changes during germination. Parallel increases in the quantity of soluble protein and GOT specific activity suggest that this isoenzyme is involved in the onion's nitrogen metabolism during germination. ' ,, ,. ,, .

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Section: Discussionmentioning

confidence: 61%

Isoenzyme Activities during the Early Stages of Allium Radicle Germination

Mallery

1972

Physiologia Plantarum

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“…Acetylcholinesterase was reported in the fruit of Green Hubbard, flavedo of three citrus firuits, and orange and lemon albedo. This activity, however, was not affected by 10-s M DFP and was slightly stimulated by 10-s M eserine (Schwartz et al, 1964). By definition, cholinesterases are inhibited by 10-s M of both DFP and eserine (Augustinsson, 1961) .…”

Section: Substrate Speciticitymentioning

confidence: 87%

“…The two esterases inhibited by organophosphorus compounds were classified as carboxylesterases INTRODUCTION ANIMAL ESTERASES have been extensively studied and classified in recent years (Augustinsson, 196 1;Anonymous, 1961), but relatively minor atten,tion has been devoted to ,the esterases of plant tissues. Studies with starch-gel electrophoresis ,indicate that &erases of plant tissues are as complex 'as esterases of animal tissues (Jooste et al, 1963;Schwartz et al, 1964). Recent reports from this laboratory show that esterases of the pea (Norgaard et al, 1968) and the carrot (Carino et al, 1968) could be classified according to their substrate and inhibitor specificities.…”

Section: Classification Of Some Esterases Of Thementioning

confidence: 99%

Classification of Some Esterases of the Green Bean (Phaseolus vulgaris L.)

Putnam

Montgomery

1969

Journal of Food Science

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SUMMARY Aqueous extracts of green beans hydrolyzed the acetyl, propionyl, and n‐butyryl esters of glycerol, phenol, sodium 2‐naphthol‐6‐sulfonate and choline. Triolein and soluble long‐chain esters of sodium 2‐naphthol‐6‐sulfonate were not hydrolyzed. Optimum esterase activity occurred at pH 7.2. Three esterases were classified by studylng the effects of the organophosphorus compounds, diethyl p‐nitrophenyl thioposphate (parathion), tetraethyl pyrophosphate (TEPP) and diisopropyl phosphorofluoridate (DEP), on the hydrolysis of nine substrates, One esterase, resistant to organophosphorus compounds, was classified as an arylesterase (EC 3. 1. 1. 2). The two esterases inhibited by organophosphours compounds were classified as carboxylesterases (EC 3. 1. 1. 1).

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“…Peroxidase has been studied in corn (McCune 1961Siegel and Galston 1967), in Nicotiana (Pandey 1967), and in Linum (Tyson and Jui 1967). Esterase isoenzyme systems have been investigated in maize by Schwartz et al (1965), and in Solanum by Schwartz et al (1964) and Desborough and Peloquin (1967), whilst Macko, Honold and Stahmann (1967) have shown developmental variation in a number of isoenzyme systems in wheat during germination and the early growth phase.…”

Section: Introductionmentioning

confidence: 99%