Purification of canine albumin by heat denaturation in a plasma bag

Evidence was obtained that both the WA and BLA crossidiotype (XId) groups are conformational antigens requiring both L and H chains and that with heat denaturation the antigens that define the XIds and antigen-binding activity are lost in parallel. In contrast, the primary structure-dependent crossreactive idiotype (CRI), PSL2, which is only weakly detected on native Wa and Bla monoclonal rheumatoid factors (mRFs), became prominently detected on the heated Wa and Bla mRFs. Heat denaturation may provide a simple method for distinguishing Ids determined by conformational antigen from primary structure-dependent Ids. In addition to heat denaturation, some acid conditions commonly used for preparation of RFs were also found to cause marked loss of Id antigen. The finding of PSL2-CRI on Bla mRF indicates that this Id is not unique to the WA XId.

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The effect of lipid on the heat denaturation of actomyosin.

NIPPON SUISAN GAKKAISHI ◽

10.2331/suisan.48.189 ◽

1982 ◽

Vol 48 (2) ◽

pp. 189-193 ◽

Cited By ~ 11

Author(s):

Iwao HAMADA ◽

Fukuji YABUNO ◽

Kohnosuke FURUMATSU ◽

Eiji NIWA

Keyword(s):

Heat Denaturation

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PREPARATION AND HEAT DENATURATION OF THE GLUTEN PROTEINS

Canadian Journal of Research ◽

10.1139/cjr31-077 ◽

1931 ◽

Vol 5 (4) ◽

pp. 389-406 ◽

Cited By ~ 5

Author(s):

W. H. Cook

Keyword(s):

Elevated Temperatures ◽

Marked Decrease ◽

Hydrogen Ion ◽

Ion Concentration ◽

Heat Denaturation ◽

Hydrogen Ion Concentration ◽

Gluten Proteins ◽

Buffer Solutions ◽

Natural Moisture Content ◽

Low Solubility

Gliadin prepared by several different methods had the same nitrogen content and distribution. The critical peptization temperature (C.P.T.) in 60% alcohol and viscosity in 30% urea-buffer solutions, however, showed considerable variation, preparations of high C.P.T. (low solubility) being more viscous. This variation in the physical properties is explained by fractionation or denaturation incidental to the method of preparation.Gluten precipitated from 30% urea solutions at salt concentrations varying from 0.1 to 0.5 of saturation, yielded fractions that varied continuously in their gliadin and glutenin content, as judged from their percentage of arginine nitrogen.Gluten dispersed in buffered 30% urea solutions showed no change in viscosity during 101 hr. after the gluten was completely dispersed. A variation of hydrogen ion concentration between pH 6.0 and 6.95 had little effect on its viscosity. Heating at 70 °C. caused a marked decrease in the viscosity of this dispersion during the first hour. When gliadin dispersions are heated as above only samples having a high initial viscosity and C.P.T. become less viscous. Heating gliadin of natural moisture content (12 to 14%) at 70 °C. for varying periods of time did not change significantly its subsequent C.P.T. and viscosity in 60% alcohol. More severe heat treatments at higher moisture contents rendered the gliadin insoluble in 60% alcohol. Dilute alcoholic extracts of heated flours contained less protein than those of unheated controls. However, the C.P.T. of the former was lower than that of the latter. It is concluded from these experiments that when the gluten proteins are subjected to elevated temperatures, the glutenin fraction is first affected, next the gliadin fractions of low solubility, and finally, under severe conditions, all of the gliadin is denatured.

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Light Scattering and Flow Dichroism Studies on DNA After the Photoreaction with Psoralen

Zeitschrift für Naturforschung B ◽

10.1515/znb-1972-0216 ◽

1972 ◽

Vol 27 (2) ◽

pp. 196-200 ◽

Cited By ~ 9

Author(s):

S. Marciani ◽

M. Terbojevic ◽

F. Dall’Acqua

Keyword(s):

Heat Treatment ◽

Molecular Weight ◽

Light Scattering ◽

Double Helix ◽

Heat Denaturation ◽

Scattering Measurements ◽

Helix Structure ◽

Double Helix Structure

Light scattering measurements performed on DNA after irradiation in the presence of psoralen clearly show that inter strand cross linkings are present in the macromolecule. In fact after heat denaturation and successive cooling irradiated macromolecule shows a molecular weight practically unchanged while a DNA sample after the same treatment shows a molecular weight half of the intact native DNA. Also the general conformation of irradiated DNA undergoes practically to no modifications after the same heat treatment while native DNA shows itself to have been strongly modified. Moreover, on the basis of flow dichroism determinations, DNA cross-linked by psoralen after heat denaturation showed to be able to restore its ordered double helix structure, during the successive cooling.

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A Case of Trisomy 8

Acta geneticae medicae et gemellologiae ◽

10.1017/s112096230002388x ◽

1974 ◽

Vol 23 (S1) ◽

pp. 253-258 ◽

Cited By ~ 3

Author(s):

B. Dallapiccola ◽

P. E. Gallenga ◽

A. Pinca ◽

L. Capra

Keyword(s):

Mental Retardation ◽

Cardiovascular System ◽

Congenital Malformations ◽

The Other ◽

Trisomy 13 ◽

Heat Denaturation ◽

Retinal Vessels ◽

Trisomy 8 ◽

Ocular Lesions ◽

The Individual

A case of 8 trisomy syndrome, identified on the basis of the heat denaturation technique, has been detected in a patient with mental retardation, congenital malformations, and peculiar ocular anomalies. This observation confirms that, even without evidence of mosaicism, this chromosome does not seriously upset the viability of cells and could be less deleterious to the individual than trisomy 13, 18, or 21.The mental development is not too much impaired and the skeletal abnormalities are mild, as compared to those found in previously reported cases. On the other hand, the cardiovascular system is involved and the ocular lesions are complex. They include prominent eyes, epicanthus, hypertelorism, antimongoloid slant of palpebral fissures, ectopia of lacrimal point, megalocornea, enlarged iridocorneal angle, subatrophic papilla, tortuosities of retinal vessels, absence of deep perception.

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Structural optimization of cyclic peptides that efficiently detect denatured collagen

Organic & Biomolecular Chemistry ◽

10.1039/c9ob01042d ◽

2019 ◽

Vol 17 (31) ◽

pp. 7380-7387 ◽

Cited By ~ 4

Author(s):

Koh K. Takita ◽

Kazunori K. Fujii ◽

Kento Ishii ◽

Takaki Koide

Keyword(s):

Structural Optimization ◽

Cyclic Peptides ◽

Heat Denaturation ◽

Mimetic Peptide

The optimized cyclic collagen-mimetic peptide effectively detects denatured collagen without prior heat-denaturation.

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Partial purification and properties of the two common inherited forms of human erythrocyte adenylate kinase

Biochemical Journal ◽

10.1042/bj1300797 ◽

1972 ◽

Vol 130 (3) ◽

pp. 797-803 ◽

Cited By ~ 15

Author(s):

C. Brownson ◽

N. Spencer

Keyword(s):

Adenylate Kinase ◽

Effect Of Temperature ◽

Partial Purification ◽

Heat Denaturation ◽

Gel Chromatography ◽

Molecular Weights ◽

Purification And Properties ◽

Increasing Temperature

1. The partial purification of adenylate kinase, types 1 and 2, from human erythrocytes is described. 2. Gel chromatography of both forms of the enzyme gave estimates of the molecular weights in the range 20000–23000. 3. Studies on crude haemolysates at various pH values indicated that the type 2 enzyme was less stable than the type 1. Heat denaturation studies on the partially purified enzymes confirmed these findings. 4. Measurements of rates of inhibition by iodoacetate and iodoacetamide showed that the type 2 enzyme reacts more readily than the type 1 enzyme with both reagents. 5. The effect of temperature on the initial velocity of ADP formation was measured at a single concentration of both AMP and MgATP2-. The two forms of the enzyme responded differently to increasing temperature.

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Hydrolysis of a naturally occurring β-glucoside by a broad-specificity β-glucosidase from liver

Biochemical Journal ◽

10.1042/bj2370469 ◽

1986 ◽

Vol 237 (2) ◽

pp. 469-476 ◽

Cited By ~ 24

Author(s):

K L LaMarco ◽

R H Glew

Keyword(s):

Guinea Pig ◽

Competitive Inhibitor ◽

Heat Denaturation ◽

Pig Liver ◽

Naturally Occurring ◽

Aryl Glycosides ◽

Beta Glucosidase ◽

Hydrolysis Of ◽

Guinea Pig Liver ◽

Broad Specificity

We have isolated from guinea-pig liver a broad-specificity beta-glucosidase of unknown function that utilizes as its substrate non-physiological aryl glycosides (e.g. 4-methylumbelliferyl beta-D-glucopyranoside, p-nitrophenyl beta-D-glucopyranoside). The present paper documents that this enzyme can be inhibited by various naturally occurring glycosides, including L-picein, dhurrin and glucocheirolin. In addition, L-picein, which acts as a competitive inhibitor of the broad-specificity beta-glucosidase (Ki 0.65 mM), is also a substrate for this enzyme (Km 0.63 mM; Vmax. 277,000 units/mg). Heat-denaturation, kinetic competition studies, chromatographic properties and pH optima all argue strongly that the broad-specificity beta-glucosidase is responsible for the hydrolysis of both the non-physiological aryl glycosides and L-picein. This paper demonstrates that beta-glucosidase can catalyse the hydrolysis of a natural glycoside, and may provide a key to understanding the function of this enigmatic enzyme. A possible role in the metabolism of xenobiotic compounds is discussed.

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