A comparative investigation of isozyme fractions separated from plant tissues

Hall, Timothy C.; McCown, Brent H.; Desborough, Sharon; McLeester, R.C.; Beck, G. Ε.

doi:10.1016/s0031-9422(00)85435-7

Cited by 25 publications

(7 citation statements)

References 15 publications

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“…tivity were common to different organs in several species (Hall et al, 1969). In a study of isoenzymes of 8-day seedlings of barley, Upadhya and Yee (1968) noted that some peroxidase isoenzymes were common to the root, coleoptile, and leaf, but variations in the banding patterns of each tissue existed.…”

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confidence: 99%

A Comparative Investigation of Peroxidases From Germinating Peanuts (Arachis Hypogaea): Electrophoresis

Thomas

Neucere

1974

American J of Botany

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Dormant seed and organs of 0‐, 1‐, 2‐, 5‐, 8‐, 11‐, and 14‐day‐old plants of Arachis hypogaea L. were homogenized in phosphate buffer and the lipid‐free extracts analyzed for benzidine and pyrogallol peroxidases using starch‐gel electrophoresis. On a wet weight basis, one weak band of benzidine peroxidase activity was detected in dormant cotyledons and three bands in 1‐day cotyledons. In 5‐day tissue, activity had increased significantly; at 14 days, the number of bands had decreased but staining intensity was maintained. In the extract from dormant axis, a single cathodic site of benzidine peroxidase activity was observed; however, on day two there was a marked increase in the number of bands and intensity of reaction in epicotyl and hypocotylradicle tissues. By day 14, the number and density of bands had decreased noticeably in the epicotyl and hypocotyl. Extracts from 14‐day roots exhibited more sites of reaction and greater intensity of staining of benzidine peroxidase than at five days of growth. Localized areas of activity at Rf ‐0.44 and ‐0.52 were present in extracts of all four organs when either benzidine or pyrogallol was used as the hydrogen donor. Although marked similarity existed between banding patterns of organs, qualitative and quantitative ontogenetic differences in peroxidases were apparent.

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A Comparative Investigation of Peroxidases From Germinating Peanuts (Arachis Hypogaea): Electrophoresis

Thomas

Neucere

1974

American J of Botany

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“…(concentrated Another nonspecific reaction, which has been previously ulfate); d: re-observed when staining for malate dehydrogenase activity formation of on polyacrylamide gels, is the appearance of sharply defined in the text. areas which do not show any background color and which ent migration have been termed "anti bands" (12). The molecular weight of one of these anti bands (AB, Fig.…”

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confidence: 99%

“…In addition to this variation in the number of malate dehydrogenase isoenzymes which have been reported even from the same plant, a number of workers have found changes in malate dehydrogenase isoenzymes during plant development (5,12,14,15,27), or that the isoenzymes are localized in specific cell organelles (3,10,19,21,22,25,28), or that they have different molecular weights (5,11,15,25). Malate dehydrogenase isoenzymes have also been used as genetic markers with plants (4,19,22,24), apparently without regard for the difficulty of obtaining reproducible identification of the isoenzymes.…”

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“…Since then more isoenzymes of malate dehydrogenase have been found in plants, and there is considerable variation in the number which have been reported for the same species. These range from three (25) to twelve (22) in maize, from two (4) to ten (24) in wheat, three (28) or four (21) in spinach, and in certain ornamental plants only one malate dehydrogenase enzyme has been detected (12). In cotton, at least three malate dehydrogenase isoenzymes have been reported (8,27), but with crude extracts of cotton plants the exact number of isoenzymes could not be ascertained (27).…”

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Malate Dehydrogenase Isoenzymes from Cotton Leaves

O'Sullivan¹,

Wedding²

1972

Plant Physiol.

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Malate dehydrogenase isolated from leaves of the cotton plant (Gossypium hirsutum L.) appears in the form of several isoenzymes. Four of the isoenzymes found in cotton leaf ex- (24) in wheat, three (28) or four (21) in spinach, and in certain ornamental plants only one malate dehydrogenase enzyme has been detected (12). In cotton, at least three malate dehydrogenase isoenzymes have been reported (8, 27), but with crude extracts of cotton plants the exact number of isoenzymes could not be ascertained (27).In addition to this variation in the number of malate dehydrogenase isoenzymes which have been reported even from the same plant, a number of workers have found changes in malate dehydrogenase isoenzymes during plant development (5,12,14,15,27), or that the isoenzymes are localized in specific cell organelles (3,10,19,21,22,25,28), or that they have different molecular weights (5,11,15,25). Malate dehydrogenase isoenzymes have also been used as genetic markers with plants (4,19,22,24), apparently without regard for the difficulty of obtaining reproducible identification of the isoenzymes.One source of interest in the study of isoenzymes is the possible correlation of physiological function with individual isoenzymes. The belief that such a separation of functions may exist for plant malate dehydrogenase stems from the observation that malate exists in two pools in the plant cell (18). Unique metabolic roles in different parts of the plant cell have been suggested (21,28,29) as well as a role in salt uptake by plants (27).The considerable confusion regarding malate dehydrogenase isoenzymes outlined above and the interest which would attach to a better understanding of these isoenzymes prompted this study of the malate dehydrogenase isoenzymes of the cotton plant. Isoenzyme is here broadly defined to include all proteins with malate dehydrogenase activity. MATERIALS AND METHODSMalate dehydrogenase (E.C. 1 . 1 .1 . 37) isoenzymes were obtained from the leaves of cotton (Gossypium hirsutum L., var. Delta Pine 16). Plants were grown in a temperaturecontrolled glasshouse (29 C maximum, 21 C min.) under natural light. Leaves from one group of 6-to 8-week-old plants were generally used. Leaves were excised, and the petioles were placed in distilled water for transport to the laboratory. Extraction commenced within 20 min.Extraction and Ammonium Sulfate Precipitation. For extraction, petioles were removed, 10 g of leaf blades were weighed and counted. The leaves were rolled and cut into pieces approximately 0.5 X 0.5 cm with a scissors. All succeeding operations were performed in the cold at 0 to 4 C.The chopped leaves were placed in an 80-ml container of a Lourdes homogenizer and sprinkled with 5.0 g of Polyclar AT. To this was added 40 ml of extraction buffer consisting of 50 mm tris-HCl, 10 mm mercapthoethanol and 1 mM EDTA at pH 7.5. Homogenization consisted of three periods of 10 sec at 60 v with 20-sec intervals. The ground slurry was squeezed through a nylon bag with a 25 X 35 threads/cm2 mesh and an addi...

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“…Isoenzymes present in seed tissue (Cherry and Ory, 1973;Macko et al, 1967) and in other plant tissues (Kadam e t al., 1973;Hall e t al., 1969) have also been resolved into distinct patterns by this technique. Isoenzymes present in seed tissue (Cherry and Ory, 1973;Macko et al, 1967) and in other plant tissues (Kadam e t al., 1973;Hall e t al., 1969) have also been resolved into distinct patterns by this technique.…”

Section: Multiple Enzyme Forms Of Tomato Seeds and Seedlingsmentioning

confidence: 99%

Multiple enzyme forms of tomato seeds and seedlings

Stein¹,

Lime²

1978

J. Agric. Food Chem.

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Proteins were extracted from dormant seeds, germinating seeds, and 12-day-old seedlings of Chico I11 and Homestead-24 tomato cultivars. Disc gel electrophoresis of the crude extracts showed that the number of enzyme forms differed with developmental stage of each cultivar. Generally the number of enzyme forms was greater in seedlings than in dormant seeds; exceptions were the numbers of enzyme forms of catalase and malic dehydrogenase, which decreased. In Homestead-24, the number of general protein forms was greater in seedlings than in dormant seeds. In Chico 111, the number of protein forms was the same in dormant seeds and seedlings. The number of protein forms was lowest a t the germinating seeds stage of both cultivars. Differences between the enzyme activities of the two cultivars were detected.Seeds contain two types of proteins: metabolic proteins, both enzymatic and structural, which are concerned with cellular activities, and a second type, the storage or reserve proteins. Many of the former exist in multiple molecular forms known as isoenzymes. The latter have no enzymatic activity (Varner, 1965; Atschul e t al., 1966). Both types of proteins function after promotion of seed germination. Reserve proteins are hydrolyzed by enzymatic proteins, and the degradation products are a source of nitrogen and carbon for the developing seedling (Oota e t al., 1953).Disc gel electrophoresis has been the most convenient method for the resolution of protein mixtures. Isoenzymes present in seed tissue (Cherry and Ory, 1973; Macko et al., 1967) and in other plant tissues (Kadam e t al., 1973; Hall e t al., 1969) have also been resolved into distinct patterns by this technique. Numerous studies of enzyme activities in tomato fruit have been reported (Lee and MacMillan, 1968; Nakagawa Food Crops Utilization Research Laboratory, Subtropical Texas Area, Southern Region, Agricultural Research Service, US. Department of Agriculture, Weslaco, Texas 78596. et al., 1970;Hobson, 1967Hobson, ,1974 and most concerned the enzymatic changes associated with ripening. Only few investigations have dealt with the identification of enzyme forms present in tomato seeds and seedlings and the changes those enzyme forms undergo during seed germination. A fundamental knowledge of the enzyme forms present in seeds and seedling would allow a better understanding of the biochemical steps that accompany the development of the plant. Any differences in enzyme distribution among varieties might enable the screening of plant crops for factors such as disease resistance and agronomic performance.We undertook to identify and compare the enzyme forms of dormant seeds, germinating seeds, and seedlings of a firm (Chico 111) and a soft (Homestead-24) variety of tomato, and to determine whether firmness of fruit could be related to the electrophoretic patterns of enzymes from plants a t an early stage of development. We investigated the enzyme forms of acid and alkaline phosphatase, esterase, catalase, peroxidase, and malic dehydrogenase (MDH). Of these,...

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A comparative investigation of isozyme fractions separated from plant tissues

Cited by 25 publications

References 15 publications

A Comparative Investigation of Peroxidases From Germinating Peanuts (Arachis Hypogaea): Electrophoresis

A Comparative Investigation of Peroxidases From Germinating Peanuts (Arachis Hypogaea): Electrophoresis

Malate Dehydrogenase Isoenzymes from Cotton Leaves

Multiple enzyme forms of tomato seeds and seedlings

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