Unusual Electrophoretic Patterns of Plasma Proteins in Human Subjects

1961 ◽  
Vol 7 (2) ◽  
pp. 107-114 ◽  
Author(s):  
Eugene L Kanabrocki
Keyword(s):  
Plasma Proteins ◽  
Human Subjects ◽  
Protein Fractions ◽  
Normal Adult ◽  
Globulin Fraction ◽  
Specific Disease ◽  
Double Peaks ◽  
Electrophoretic Patterns ◽  
Beta Globulin

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.

scholarly journals PLASMA PROTEIN METABOLISM—ELECTROPHORETIC STUDIES

1945 ◽  
Vol 81 (5) ◽  
pp. 515-537 ◽  
Author(s):  
L. J. Zeldis ◽  
E. L. Alling
Keyword(s):  
Plasma Protein ◽  
Plasma Proteins ◽  
Blood Stream ◽  
Human Albumin ◽  
Electrophoretic Patterns ◽  
Dog Plasma ◽  
Beta Globulin ◽  
Veronal Buffer ◽  
Protein Components ◽  
High Beta

Electrophoretic patterns of normal dog plasma in veronal buffer at pH 8.5 are shown to be essentially similar to patterns of human plasma. Dog albumin has a higher mobility than human albumin and in a mixture of dog and human plasmas migrates as a partially separated peak. Normal dog plasma frequently shows four alpha globulin peaks. Rates of restoration of plasma protein components in dogs subjected to acute plasmapheresis have been studied by electrophoresis. During the first 24 hours following such acute depletion, appreciable quantities of all electrophoretic components of the plasma proteins enter the circulating blood stream even when food is not given and has not been given for 12 hours before plasmapheresis. In such fasting periods albumin and total globulin appear in approximately the proportions present in normal plasma. Alpha and beta globulins continue relatively elevated during subsequent days in which caloric and protein intakes are adequate for weight and nitrogen gains. Initial albumin levels, however, are regained more slowly than those of total globulin. The relative proportions of the electrophoretic components of plasma proteins may be disturbed from normal following a single acute depletion for as long as 2 to 3 weeks after the total protein level has returned to normal. Abnormally high beta globulin and fibrinogen, but a low albumin, were found in a dog with an acute and chronic cholangitis and hepatitis. Similar elevation of gamma globulin was noted in a dog in which a hemolytic reaction occurred.

TRANSPORT OF CHORIONIC GONADOTROPHIN (HCG) IN BLOOD

1961 ◽  
Vol 36 (3) ◽  
pp. 438-442
Author(s):  
D. Nagy ◽  
I. Gáti ◽  
G. Keller
Keyword(s):  
Chorionic Gonadotrophin ◽  
Globulin Fraction ◽  
Preparative Electrophoresis ◽  
Beta Globulin

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.

EFFECT OF THE ORAL ADMINISTRATION OF GLUCOSE UPON THE CONCENTRATION OF SERUM AMYLASE IN NORMAL ADULT HUMAN SUBJECTS

1949 ◽  
Vol 159 (1) ◽  
pp. 29-32 ◽  
Author(s):  
Norman P. Goldstein ◽  
Benjamin W. Smith ◽  
Jerome H. Epstein ◽  
Joseph H. Roe
Keyword(s):  
Oral Administration ◽  
Serum Amylase ◽  
Human Subjects ◽  
Normal Adult ◽  
Adult Human

Imprecision of quantification of serum protein fractions by electrophoresis on cellulose acetate.

1986 ◽  
Vol 32 (2) ◽  
pp. 356-357 ◽  
Author(s):  
S N Kahn ◽  
L P Strony
Keyword(s):  
High Resolution ◽  
Serum Albumin ◽  
Cellulose Acetate ◽  
Serum Protein ◽  
Protein Fractions ◽  
Visual Interpretation ◽  
Cellulose Acetate Electrophoresis ◽  
Trained Observer ◽  
Electrophoretic Patterns

Abstract We studied the precision of densitometric quantification of the protein zones resolved by cellulose acetate electrophoresis. Replicate analyses of patients' samples by a single technologist showed mean CVs ranging from 2.9% for serum albumin to 9.5% for alpha 1-globulin. There were marked differences in measurements obtained by replicate analysis of the same samples by two experienced technologists. We calculated what changes in fractional concentrations would be analytically significant and concluded that densitometry of cellulose acetate electrophoretograms can only be semi-quantitative. We suggest that visual interpretation of high-resolution electrophoretic patterns by a trained observer can replace densitometry in most cases.

scholarly journals THE USE OF RADIOACTIVE LYSINE IN STUDIES OF PROTEIN METABOLISM

1949 ◽  
Vol 90 (4) ◽  
pp. 297-313 ◽  
Author(s):  
L. L. Miller ◽  
W. F. Bale ◽  
C. L. Yuile ◽  
R. E. Masters ◽  
G. H. Tishkoff ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Protein Metabolism ◽  
Plasma Proteins ◽  
The Body ◽  
Globulin Fraction ◽  
Red Cell ◽  
Turnover Rates ◽  
High Concentration ◽  
Plasma Albumin ◽  
Lysine Residues

Racemic lysine labeled with C14 in the epsilon carbon position was fed to dogs. The distribution of C14 in blood and tissue fractions is recorded. In normal dogs sacrificed at 24 hours, approximately one-third of the C14 was found in the urine, one-third in expired air, and one-third in the body, mostly in protein, predomantly as lysine residues. The rate of C14 excretion as CO2, hour by hour, paralleled closely the amount of non-protein C14 in the blood plasma. The liver, kidney, pancreas, and spleen all have high values for C14 in 24 hour and 17 day experiments. The gastrointestinal tract is significantly high in the 24 hour experiments. Plasma protein from animals previously fed C14 containing lysine and thus in turn labeled, was transfused into other dogs and the rate of disappearance of albumin and globulin fractions from the circulation of the recipient dog followed. The results lead to the conclusion that as a whole, plasma proteins are utilized and replaced at a rate of at least 10 per cent per 24 hours. This minimum rate is substantially faster than turnover rates commonly accepted and emphasizes the rôle played by the plasma proteins in the protein economy of the body. The exact rate determination is made uncertain by the lack of knowledge of the magnitude of the amount of protein in solution in extracellular and lymph spaces and its rate of equilibrium with circulating plasma proteins. Evidence from these transfusion studies indicates that plasma globulin is metabolized at a significantly faster rate than plasma albumin. This is confirmed by the observation that following the feeding of labeled lysine to dogs, C14 is first incorporated in globulin in high concentration but that later it also disappears more rapidly from the globulin fraction. These data suggest that the period of bone marrow maturation of the red cell during which time its related hemoglobin is synthesized does not exceed 3 to 5 days.

Distribution of plasma proteins and hyaluronic acid in synovial fluid and serum of human subjects in hydarthrosis

1974 ◽  
Vol 55 (2) ◽  
pp. 205-209 ◽  
Author(s):  
Jacques R. Poortmans ◽  
Jean-Jacques S'jongers ◽  
Georges Bidon
Keyword(s):  
Hyaluronic Acid ◽  
Synovial Fluid ◽  
Plasma Proteins ◽  
Human Subjects

scholarly journals Blood plasma proteins and protein fractions in roe deer Capreolus capreolus L.

2015 ◽  
Vol 16 (3) ◽  
pp. 289-298
Author(s):  
Dorota CYGAN-SZCZEGIELNIAK ◽  
Karolina STASIAK ◽  
Bogdan JANICKI ◽  
Aleksandra Roslewska ◽  
Magdalena STANEK
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Roe Deer ◽  
Capreolus Capreolus ◽  
Protein Fractions ◽  
Blood Plasma Proteins

Generation of prothrombin-R with plasma protein fractions

1962 ◽  
Vol 202 (4) ◽  
pp. 664-670 ◽  
Author(s):  
Marion I. Barnhart ◽  
B. C. Das
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Specific Activity ◽  
Active Agent ◽  
Deae Cellulose ◽  
Protein Fractions ◽  
Beta Globulin ◽  
Plasma Fractions ◽  
Complete Regeneration ◽  
Prothrombin Activation

An activity of blood concerned in prothrombin activation is reported that was not previously recognized. Prothrombin-R was produced from a prothrombin derivative prepared with lysosomes after addition of various plasma fractions. The reaction was optimal at pH 7.9, and thrombin-C was not formed. Cohn fractions from either rabbit or human plasma generated prothrombin-R, although only fraction IV (alpha globulin plus) gave complete regeneration. Further purification of Cohn fractions was achieved with DEAE-cellulose chromatography. All fractions gave 100% yield of prothrombin-R. An immunoelectrophoretically pure alpha globulin had the highest specific activity. Partially purified gamma or beta globulin and albumin, also, were effective in that order. Immunologic data support the view that the alpha globulin content of these other fractions was responsible for generation of prothrombin-R. Most likely the active agent is an enzyme. Accordingly the plasma constituent which generates prothrombin-R is designated enzyme-R.

Electrophoretic patterns of the plasma proteins in diffuse liver necrosis

1956 ◽  
Vol 30 (6) ◽  
pp. 882-893 ◽  
Author(s):  
Bernardo Léo Wajchenberg ◽  
Gunter Hoxter ◽  
Jayme Segal ◽  
Emilio Mattar ◽  
A.B. de Ulhoa Cintra ◽  
...  
Keyword(s):  
Plasma Proteins ◽  
Liver Necrosis ◽  
Electrophoretic Patterns
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