TRANSPORT OF CHORIONIC GONADOTROPHIN (HCG) IN BLOOD

1961 ◽  
Vol 36 (3) ◽  
pp. 438-442
Author(s):  
D. Nagy ◽  
I. Gáti ◽  
G. Keller

ABSTRACT It has been shown by preparative electrophoresis that in the pregnancy serum HCG is transported in the beta globulin fraction. The linkage is believed to be adsorptive in nature.

1961 ◽  
Vol 7 (2) ◽  
pp. 107-114 ◽  
Author(s):  
Eugene L Kanabrocki

Abstract Study of 313 plasma electrophoretic patterns from 158 hospitalized subjects revealed that 30 per cent of these patients exhibited a heterogeneity marked by occurrence of double peaks in the alpha-2 and 6 per cent in the beta globulin fraction. Occurrence of double peaks could not be related to any specific disease. Similar study of plasma from 18 normal adult subjects did not reveal double peaks in any of the protein fractions. Existence of prealbumin components, with mobilities greater than that of the albumin, has been observed in 6 of 158 pathological subjects. Mobilities and concentrations of components x1, x2, and x3 are reported.


1967 ◽  
Vol 55 (4) ◽  
pp. 587-599 ◽  
Author(s):  
A. Burger ◽  
R. Kunz

ABSTRACT Thyroid stimulating activity was demonstrated in human urinary chorionic gonadotrophin preparations (HCG) by the method of McKenzie (1958). The biological response of the material was similar to that of bovine pituitary thyrotrophin (TSH), but no neutralization of the activity occurred with antibodies against human pituitary TSH and, even more interesting, with antibodies against human urinary chorionic gonadotrophin preparations. The latter antibodies perfectly neutralized human pituitary TSH. The Gamma-G-globulins precipitated from a mixture of HCG and anti-HCG contained biological activity whereas no activity was recovered in the Gamma-G-globulin fraction when HCG was mixed with non immune rabbit serum. This may indicate the presence of a soluble antigen-antibody complex.


1964 ◽  
Vol 29 (3) ◽  
pp. 263-271 ◽  
Author(s):  
G. ILLEI ◽  
PAMELA M. MORITZ

SUMMARY Antisera were raised to human chorionic gonadotrophin (HCG) and human menopausal gonadotrophin (HMG). Normal human serum and human pituitary and chorionic gonadotrophins reacted with both antisera in immunological experiments. After absorption with human serum, the γ-globulin fractions of the antisera were isolated, and only the reaction to the hormone preparations remained. Immunoelectrophoresis revealed a common antigenic factor in the α2-β globulin region. The γ-globulin fraction of HCG antiserum seems to be suitable for the assay of HCG, while that of the HMG antiserum might be employed for the detection of HMG.


1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.


1963 ◽  
Vol 43 (1) ◽  
pp. 155-160
Author(s):  
Jørgen Falck Larsen ◽  
Christian Hamburger

ABSTRACT Various modifications of the Parlow test for luteinizing hormone (ovarian ascorbic acid depletion in rats) were tried. Human chorionic gonadotrophin was used instead of hypophyseal luteinizing hormone. The precision of the method was found to be so low, however, that the test could not be used for routine clinical analysis. The low precision found in this and other laboratories is thought to be due to the strains of rats used.


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