scholarly journals ANTIGENIC PROPERTIES OF NATIVE AND REGENERATED HORSE SERUM ALBUMIN

1943 ◽  
Vol 78 (1) ◽  
pp. 1-8 ◽  
Author(s):  
John O. Erickson ◽  
Hans Neurath
Keyword(s):  
Serum Albumin ◽  
Protein Denaturation ◽  
Horse Serum ◽  
Native State ◽  
Immunological Activity ◽  
Denatured Protein ◽  
Antigenic Activity ◽  
Antigenic Properties ◽  
The Mean ◽  
Physical And Chemical

Comparative immunological measurements have been carried out on crystalline horse serum albumin in the native state and after regeneration from 8 M urea solutions. The mean antigenic activity of the regenerated protein has been found to be less than 10 per cent of that of the native, whereas both antigens proved to be immunologically equivalent. The problem of the relation between protein denaturation and immunological activity has been considered and discussed on the basis of known physical and chemical differences between native and denatured protein.

The Antigenic Properties of Native and Regenerated Horse Serum Albumin

Science ◽  
1942 ◽  
Vol 96 (2483) ◽  
pp. 116-117
Author(s):  
Hans Neurath ◽  
John O. Erickson ◽  
Gerald R. Cooper
Keyword(s):  
Serum Albumin ◽  
Horse Serum ◽  
Antigenic Properties

scholarly journals IMMUNOCHEMICAL PROPERTIES OF NATIVE AND DENATURED HORSE SERUM GLOBULINS

1945 ◽  
Vol 28 (5) ◽  
pp. 421-448 ◽  
Author(s):  
John O. Erickson ◽  
Hans Neurath
Keyword(s):  
Horse Serum ◽  
Guanidine Hydrochloride ◽  
Specific Effect ◽  
Cross Reactivity ◽  
Type I ◽  
Serum Globulin ◽  
Antigenic Activity ◽  
Order Of Magnitude ◽  
The Mean ◽  
Mean Molecular Weight

1. The influence of guanidine hydrochloride on the denaturation and regeneration of Type I antipneumococcal horse serum globulin was determined by measurements of viscosity, diffusion, and sedimentation in the ultracentrifuge. In addition, the effect of NaCNS on the antibody globulin was studied. 2. Both the irreversibly denatured and the regenerated fractions were found to be precipitable by SI. The observed changes in combining ratio have been tentatively explained in terms of (a) changes in the mean molecular weight, or alternatively (b) an increase in the number of serologically active groups upon denaturation, followed by masking of the latter upon regeneration. Discounting a specific effect of NaCNS on either fraction, the extent of specific precipitation is of the same order of magnitude for native and irreversibly denatured antibody. 3. Quantitative precipitin titrations have been performed on rabbit antisera to native and irreversibly denatured horse antibody, and normal globulin GI, respectively. No significant differences in the antigenic activity of these proteins were found. Measurements of their cross-reactivity led to the conclusion that the native and irreversibly denatured fractions of antibody globulin are antigenically more closely related to each other than to the corresponding fractions of normal globulin, and vice versa.

scholarly journals THE ANTIGENIC PROPERTIES OF NATIVE AND REGENERATED HORSE SERUM ALBUMIN

Science ◽  
1942 ◽  
Vol 96 (2483) ◽  
pp. 116-117 ◽  
Author(s):  
H. NEURATH ◽  
J. O. ERICKSON ◽  
G. R. COOPER
Keyword(s):  
Serum Albumin ◽  
Horse Serum ◽  
Antigenic Properties

scholarly journals SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS

1936 ◽  
Vol 19 (3) ◽  
pp. 427-438 ◽  
Author(s):  
A. E. Mirsky ◽  
M. L. Anson
Keyword(s):  
Serum Albumin ◽  
Quantitative Methods ◽  
Protein Denaturation ◽  
Protein Molecule ◽  
Insoluble Fraction ◽  
Egg Albumin ◽  
Sh Groups ◽  
Denatured Protein ◽  
Hydrolyzed Protein ◽  
Air Water Interface

1. In native egg albumin no SH groups are detectable, whereas in completely coagulated albumin as many groups are detectable as are found in the hydrolyzed protein. In egg albumin partially coagulated by heat the soluble fraction contains no detectable groups, and the insoluble fraction contains the number found after hydrolysis. 2. In the reversal of denaturation of serum albumin, when insoluble protein regains its solubility, S-S groups which have been detectable in the denatured protein, disappear. 3. When egg albumin coagulates at an air-water interface, all the SH groups in the molecule become detectable. 4. In egg albumin coagulated by irradiation with ultraviolet light, the same number of SH groups are detectable as in albumin coagulated by a typical denaturing agent. 5. When serum albumin is denatured by urea, there is no evidence that S-S groups appear before the protein loses its solubility. 6. Protein denaturation is a definite chemical reaction: different quantitative methods agree in estimates of the extent of denaturation, and the same changes are observed in the protein when it is denatured by different agents. A protein molecule is either native or denatured. The denaturation of some proteins can be reversed.

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diethyl Ether ◽  
Bovine Serum ◽  
Domestic Fowl ◽  
Laying Hens ◽  
Peripheral Plasma ◽  
The Mean ◽  
Precision And Accuracy ◽  
Chicken Ovary

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.

CHEMISTRY OF GONADOTROPHINS IN RELATION TO THEIR ANTIGENIC PROPERTIES

1969 ◽  
Vol 62 (1_Suppl) ◽  
pp. S13-S30 ◽  
Author(s):  
W. R. Butt
Keyword(s):  
Biological Activity ◽  
Guinea Pigs ◽  
Complement Fixation ◽  
Neuraminic Acid ◽  
Fixation Technique ◽  
Immunological Activity ◽  
Antigenic Properties ◽  
Specific Antisera ◽  
Structural Differences

ABSTRACT Several chemical differences between FSH, LH and HCG have been reported: thus LH and HCG are richer in proline than FSH and FSH and HCG contain more N-acetyl neuraminic acid than LH. Sub-units of LH are formed by treatment with urea, guanidine or acid. HCG also may contain two sub-units. The sub-units from LH are biologically inert but retain their immunological activity: biological activity is restored when the sub-units are incubated together. There is much evidence from chemical and enzymic reactions that antigenic groups are distinct from those parts of the molecule essential for biological activity. N-acetyl neuraminic acid and probably other carbohydrates in FSH and HCG are not involved in immunological activity but are necessary for biological activity. Histidine, methionine and possibly cysteine appear to be essential for biological but not immunological activity of FSH, while tryptophan and possibly tyrosine are not essential for either. A few highly specific antisera to gonadotrophins have been prepared in rabbits and guinea pigs to crude antigens: there is no evidence that purified antigens are more likely to produce specific antisera. Differences in the immunological reactivities of urinary compared with pituitary gonadotrophins have been observed both by radioimmunoassay and by the complement fixation technique. The latter may be particularly useful for detecting structural differences in the hormones.

scholarly journals ABSENCE OF METHIONINE IN CRYSTALLINE HORSE SERUM ALBUMIN

1941 ◽  
Vol 141 (3) ◽  
pp. 999-1000
Author(s):  
Erwin Brand ◽  
Beatrice Kassell
Keyword(s):  
Serum Albumin ◽  
Horse Serum
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