Determination of protein by a modified Lowry procedure in the presence of some commonly used detergents

Cadman, Evelyn; Bostwick, J. Robert; Eichberg, Joseph

doi:10.1016/0003-2697(79)90548-7

Cited by 112 publications

(38 citation statements)

References 7 publications

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“…Концентрацию протеина определяли ме-тодом Лоури с использованием 1%-го раство-ра DSNa для солюбилизации мембран [21]. Для демаскирования латентной АТРазной активно-сти мембраны предварительно инкубировали с 0,2%-ым дигитонином (1 мг детергента/1 мг протеи на = 1/1) при 23 °С 15 мин в среде, со-держащей: 30 мМ трис-НСl (рН 7,54), 0,16 М сахарозу, 2 мг/мл протеина, 2 мг/мл дигитони-на в соответствии с методическими принципа-ми, применяемыми ранее [22,23].…”

Section: материалы и методыunclassified

The influence of iron ions on ATP-hydrolases activity of cell membranes of rat colon smooth muscle and kidney

Aa¹

2015

Ukr.Biochem.J.

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Section: материалы и методыunclassified

The influence of iron ions on ATP-hydrolases activity of cell membranes of rat colon smooth muscle and kidney

Aa¹

2015

Ukr.Biochem.J.

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“…In addition to the ras peptides, we examined four pairs of peptides that shared common amino acid sequences: peptides 33 and 34 (v-myc, residues 389-403 and 395-405), peptides 27 and 28 (v-fes residues, 893-905 and 901-913), peptides 19 and 20, (v-myb, residues 168-186 and 170-185), and peptides 21 and 22 (v-myb, residues 247-260 and 247-265) as shown in Table 2. All of these peptides induced antibodies reactive with the immunizing peptides.…”

Section: R-h-s-t-s-s-s-e-q-e-r-e-g-g-rmentioning

confidence: 99%

Efficient generation of antibodies to oncoproteins by using synthetic peptide antigens.

Tanaka¹,

Slamon²,

Cline³

1985

Proc. Natl. Acad. Sci. U.S.A.

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To examine the efficiency of generating protein-reactive antipeptide antibodies, 35 peptides encoded by retroviral or cellular oncogenes were used to immunize rabbits.Thirty-two peptides elicited antipeptide antibodies, of which 56% reacted with their respective oncoproteins. The length of the immunizing peptide was an important factor in generating antibodies reactive with native protein. Similar peptides differing in a single or a few amino acids could elicite antisera of markedly different reactivities.

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“…Protein concentrations were determined using the procedure of Cadman et al [14] with bovine serum albumin as the standard.…”

Section: Methodsmentioning

confidence: 99%

Purification and Properties of a Nucleoside Triphosphatase from Sinclair Swine

Williams¹

1984

Enzyme

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A nonspecific nucleoside triphosphatase was partially purified from skin and cutaneous melanoma tumors from Sinclair swine using chloroform precipitation, hydrophobic, ion-exchange and affinity chromatography techniques. The enzyme was not stimulated by Na^+, K^+ or Mg^2+ but it was inhibited by EDTA. The enzyme was not inhibited by quercetin, proflavin, azide or ovabain. The enzyme exhibited optimal activity over a pH range of 8-9 and the activation energy was 10.4 and 9.8 kcal/mol for dUTP and ATP, respectively. The apparent K(m) of the enzyme for dUTP and dTTP was approximately 20 µmol/l while the apparent K(m) for dATP, ATP, dCTP, CTP and UTP was in the range of 65-80 µmol/l.

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Determination of protein by a modified Lowry procedure in the presence of some commonly used detergents

Cited by 112 publications

References 7 publications

The influence of iron ions on ATP-hydrolases activity of cell membranes of rat colon smooth muscle and kidney

The influence of iron ions on ATP-hydrolases activity of cell membranes of rat colon smooth muscle and kidney

Efficient generation of antibodies to oncoproteins by using synthetic peptide antigens.

Purification and Properties of a Nucleoside Triphosphatase from Sinclair Swine

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