The purification and properties of Neurospora malate dehydrogenase

Munkres, Kenneth D.; Richards, Frederic M.

doi:10.1016/0003-9861(65)90391-7

Cited by 236 publications

(53 citation statements)

References 42 publications

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“…Total soluble protein in the seed extract was determined by the biuret method as modified by Munkers and Richards (22). Portions of the extract were precipitated with 10% trichloroacetic acid, washed with ethanol, dried, and dissolved in 1 M NaOH for biuret analysis.…”

Section: Methodsmentioning

confidence: 99%

Studies of Storage Proteins of Higher Plants

Hague¹

1975

Plant Physiol.

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Concanavalin A, the lectin of the Jack bean, Canavalia ensiformis, was extracted and compared with homologous proteins from Canavalia gladiata and Canavalia maritima. All proteins were bound to Sephadex G-100 and eluted from the gel with buffered glucose solution. Quantitative recoveries indicated that large quantities (23 to 28% of dry seed protein) of these lectins are svnthesized by all three species. Antibody preparations made against C. ensiformlis lectin failed to discriminate among the three proteins; the pattern of the precipitin bands indicated identical antigenic determinants in the Ouchterlony doublediffusion assay. Native and sodium dodecyl sulfate polyacrylamide gel electrophoresis also failed to distinguish differences in the proteins. The storage protein active in carbohydrate binding is composed, in each case, of identical subunits. However, the amino acid composition of the subunit chains from the three sources is not identical. In particular, the lectins from C. ensiforrnis and C. gladiata contain two methionine residues per protein subunit, while only one methionine residue is found in the C. martima lectin. Cyanogen bromide cleavage of the puri. fied subunit from C. maritimtia yieded two fragments with molecular weights estimated at 20,400 and 4,600, respectively. Amino acid analysis of the separated fragments indicated that the methionine residue at position 130 in C. ensiformis is absent in the lectin from C. maritima.During seed germination storage proteins are hydrolyzed, and the amino acids are transported into the growing seedling axis. However, certain storage proteins, called lectins and found largely in the cotyledons of legumes, have the capacity to bind specific carbohydrates. The functional significance of this property is unknown, but there have been several reports indicating that lectins have an affinity for the cell surface of species of Rhizobium and may, therefore, facilitate the entry of these symbiotic, nitrogen-fixing organisms into the root cortex (8,18).Relatively little is known about the mechanism of higher plant protein synthesis in comparison to that of microorganisms and animal tissues (38). A cell-free system from higher

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Section: Methodsmentioning

confidence: 99%

Studies of Storage Proteins of Higher Plants

Hague¹

1975

Plant Physiol.

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“…As a control for tissue specificity, extract was also prepared from heart muscle. The crude extract was concentrated by ultrafiltration (Amicon, Lexington, MA; 10 kD cutoff filter) to about 16 mg proteidml, as measured by the microbiuret reaction (Munkres and Richards, 1965) and cast in a sheet of polymerized collagen prepared as described above at a concentration of about 3-4 mg extract proteidml collagen. The collagen was frozen on Teflon, lyophilized, and stored at -70°C until use.…”

Section: Muscle Extractmentioning

confidence: 99%

Enhancement of skeletal muscle regeneration

Bischoff

Heintz

1994

Developmental Dynamics

161

103

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We have studied the effect of adding extra satellite cells or soluble factors from crushed muscle on regeneration of minced fragments from rat tibialis muscle. The muscle mince was wrapped in an artificial epimysium to prevent adhesions and cell immigration from adjacent muscles. Regeneration was quantitatively assessed by electrophoretic determination of the muscle-specific form of creatine kinase. Control minces exhibited three periods of change in creatine kinase activity during a 7-week regeneration period. Activity fell rapidly during the first week, then rose gradually from 1 3 weeks and increased more rapidly from 3-7 weeks. To augment the original complement of myogenic cells, satellite cells were isolated from the contralateral muscle, purified by density gradient centrifugation, and expanded in culture for 3 days before adding to the muscle mince. The added cells resulted in a 3-fold enhancement of creatine kinase activity throughout the regeneration period. Soluble muscle extract incorporated into a collagen matrix also stimulated regeneration when added to muscle mince. The extract accelerated the rate of creatine kinase increase during the 1 3 week period beyond that observed in the control or cell augmented mince, suggesting that factors in the extract may facilitate revascularization or reinnervation. The specific activity of creatine kinase was increased in regenerates augmented with both cells and extract, indicating that the effects enhance primarily myogenic processes.

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“…Protein was determined using the microbiuret procedure [12] with bovine serum albumin as a standard. The binding assays were conducted in 80/zl of 50 mM Tris-HC1 buffer, pH 7.0, with 5 mM dithiothreitol (DTT) and 50 to 200/~g of membrane protein.…”

Section: Binding Of Acp On Membrane Vesicles Of E Colimentioning

confidence: 99%

Membrane‐binding sites for acyl carrier protein in Escherichia coli

Bayan

Therisod

1989

FEBS Letters

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We report that membrane vesicles of Escherichia coli contain protein-binding sites for acyl carder protein. Scatchard analysis of the binding indicates a dissociation constant around 0.35/tM and a maximum number of protein-binding sites around 50 pmol per mg of membrane protein. Binding is on the inner membrane while the outer membrane is devoid of binding sites. These results are consistent with the fact that some aeyl carder protein-dependent enzymes implicated in phospholipid-and membrane-derived oligosaceharide biosynthesis are localized in the cytoplasmic membrane.

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The purification and properties of Neurospora malate dehydrogenase

Cited by 236 publications

References 42 publications

Studies of Storage Proteins of Higher Plants

Studies of Storage Proteins of Higher Plants

Enhancement of skeletal muscle regeneration

Membrane‐binding sites for acyl carrier protein in Escherichia coli

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