Purification and Properties of Apple Fruit Malic Enzyme

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Purification and properties of apple fruit malic enzyme.

Malic enzyme was isolated and purified from mature apple fruits (Malus sylvestris, Miller) by utilizing procedures probably applicable to other soluble enzymes in this and similar tissues.The physical properties of apple fruit malic enzyme are similar to those reported for malic enzyme from other plant and animal sources. It is specific for l-malate, TPN and requires a divalent cation for activ...

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Purification and Properties of Apple Fruit Malic Enzymel

Summarwy. \ialic enzyme wxas iso)latedl and plurifie(l froimi mature apple fruits (ainus svivcstris, Miller ) by utilizing proce(lures prol)al)ly applicable to other soluble enzymes in this and similahr tissues. The physical properties of apple fruit iinalic enzymle are similar to those reported for malic enzyme fromn other plant and( animilal sources. It is specific for L-malate, TPN and requi...

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Cultivar and fruit size influence bruise susceptibility and some physical properties of apple fruit

ABSTRACT- For most fruit types, including apples, bruising is the most common type of postharvest mechanical injury. Bruise susceptibility was investigated in 3 commercial cultivars (‘JazzTM’, ‘Granny Smith’ and ‘Fuji’) and among a range of 4 different fruit sizes (commercial counts of 135, 120, 100, and 88) in each cultivar. Bruising was carried out by dropping a uniform round steel ball (110g...

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Nicotinamide adenine dinucleotide phosphate-malic enzyme of rat liver. Purification, properties, and immunochemical studies.

Rat liver malic enzyme (EC 1.1.1.40) was purified from livers of rats fasted and refed a high sucrose diet containing 1% desiccated thyroid powder. The purification was accomplished by a six-step procedure. The specific activity of the purified enzyme was increased 181-fold above that of the initial high speed supernatant of liver extracts. Slight additional purification of malic enzyme was ach...

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Malic dehydrogenase. 8. Large scale purification and properties of supernatant pig heart enzyme.

A reproducible procedure for the large scale purification of pig heart supernatant malate dehydrogenase which yields up to 400 mg of homogeneous protein has been developed. The purity of the isolated enzyme is shown by acrylamide gel electrophoresis over a pH range from 4.9 to 9.2 as well as by detailed analysis of boundary spreading during sedimentation velocity experiments. Three enzymically ...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1966

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.41.2.214