The tritlum labeling of small amounts of protein for analysis by electrophoresis on sodium dodecyl sulfate-polyacrylamide slab gels

Kumarasamy, Ramasamy; Symons, Robert H.

doi:10.1016/0003-2697(79)90739-5

Cited by 54 publications

(12 citation statements)

References 16 publications

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“…Radiometric assays for protein hydrolysis were carried out as described by Kitch and Murdock (1986). The substrate consisted of 0.4 Ci/ml [ 3 H]methemoglobin (Kumarasamy and Symons 1979) and 2 mg/ml of unlabeled methemoglobin. Reactions were initiated by the addition of 50 l of enzyme, diluted in buffer, to 50 l of substrate solution in a 1.5-ml centrifuge tube.…”

Section: Methodsmentioning

confidence: 99%

The Role of Protease Inhibitors and Parasitoids on the Population Dynamics ofSitotroga cerealella(Lepidoptera: Gelechiidae)

Shukle

2003

Environ Entomol

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Section: Methodsmentioning

confidence: 99%

The Role of Protease Inhibitors and Parasitoids on the Population Dynamics ofSitotroga cerealella(Lepidoptera: Gelechiidae)

Shukle

2003

Environ Entomol

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“…To determine whether the percentage of ectodermal ECM components adsorbed to plastic was the same for each region, equal amounts of extracted ECM protein from each region were radioactively labeled by reductive methylation with (3H)KBH4 (Kumarasamy and Symons, 1979) and a known number of cpm were placed into each 10-pl microwell under conditions identical to those in the attachment assays. Subsequently, each well was rinsed four times with Tyrode's buffer, the rinses were pooled, scintillation fluor was added, and the solution was counted in a Packard Tri-Carb scintillation counter.…”

Section: Preparation Of Cell Substratesmentioning

confidence: 99%

Attachment of neural crest cells to endogenous extracellular matrices

Brauer

Markwald

1987

Anat. Rec.

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Newly emerging neural crest (NC) cells will enter either the lateral pathway under the surface ectoderm or the vental pathway along the neural tube depending on the axial level (Pratt et al.: Dev. Biol., 44:298-305, 1975; Thiery et al.: Dev. Biol., 93:324-343, 1982; Newgreen et al.: Cell Tissue Res., 221:521-549, 1982; LeDouarin et al.: In: The Role of Extracellular Matrix in Development. Alan R. Liss, Inc., New York, pp. 373-398, 1984; Brauer et al.: Anat. Rec., 211:57-68, 1985). A number of studies have shown a correlation between the type of extracellular matrix (ECM) associated with adjacent tissues (e.g., ectoderm, neural tube, and mesoderm) and the initial pathway taken by NC cells. Our working hypothesis is that the direction of NC cell migration (ventral vs. lateral pathway) depends on the composition of the ECM associated with the surface ectoderm and its ability to support NC cell attachment. In this study, we tested this hypothesis by isolating endogenous ECM associated with the ectoderm of each region and examining the ability of each endogenous ECM to support cranial and trunk NC cell attachment in vitro. Results indicated that both cranial and trunk NC cells preferentially attached to cranial ectodermal ECM as compared to trunk ectodermal ECM. The differences in NC cell attachment were not due to a preferential adsorption of cranial ectodermal ECM onto the ECM-conditioned plastic substrate over trunk ectodermal since approximately equal amounts of ECM bound to the plastic. These results supported the hypothesis and provide evidence that endogenous ectodermal ECM may be one factor potentially responsible for directing the NC cells along a ventral or a lateral pathway.

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“…RNA concentrations were determined by assuming that 1 mg of RNA per ml had an A260 of 24. Purified proteins were labeled in' vitro with [3H]potassium borohydride by the method of Kumarasamy and Symons (17). Gels containing radioactive proteins were prepared for fluorography by the method of Bonner and Laskey (6) and placed in light-tight presses with Kodak X-Omat XAR-5 film; the film was exposed for various times at -800C.…”

Section: Methodsmentioning

confidence: 99%

Synthesis and localization of a development-specific protein in sclerotia of Sclerotinia sclerotiorum

Russo¹,

Etten²

1985

J Bacteriol

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A development-specific protein (SSP) makes up about 35 to 40% of the total protein in sclerotia of the fungus Sclerotinia sckerotiorum. The protein consists of three charge isomers, with one isomer making up 80 to 90% of the total. In vitro translation of poly(A)+ RNA isolated from cells in early stages of sclerotia formation revealed that 44% of the amino acids incorporated was into SSP. In vivoand in vitro-synthesized forms of SSP migrated at identical rates on both isoelectric focusing and denaturing polyacrylamide gels, indicating that SSP was not synthesized as a larger precursor. This was significant because SSP accumulated in membrane-bound, organellelike structures which resemble protein bodies found in seeds of many higher plants.

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The tritlum labeling of small amounts of protein for analysis by electrophoresis on sodium dodecyl sulfate-polyacrylamide slab gels

Cited by 54 publications

References 16 publications

The Role of Protease Inhibitors and Parasitoids on the Population Dynamics ofSitotroga cerealella(Lepidoptera: Gelechiidae)

The Role of Protease Inhibitors and Parasitoids on the Population Dynamics ofSitotroga cerealella(Lepidoptera: Gelechiidae)

Attachment of neural crest cells to endogenous extracellular matrices

Synthesis and localization of a development-specific protein in sclerotia of Sclerotinia sclerotiorum

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