scholarly journals IMMUNOCHEMICAL RELATION OF BENCE-JONES PROTEINS TO NORMAL SERUM PROTEINS

1955 ◽  
Vol 216 (1) ◽  
pp. 103-111
Author(s):  
H.F. Deutsch ◽  
C.H. Kratochvil ◽  
Arnold E. Reif
Keyword(s):  
Serum Proteins ◽  
Normal Serum ◽  
Bence Jones Proteins

The absence of normal serum proteins in lymphoma patients revealed by disc electrophoresis

1969 ◽  
Vol 25 (7) ◽  
pp. 747-748 ◽  
Author(s):  
S. R. Rohlfing ◽  
E. R. Brown ◽  
S. O. Schwartz ◽  
R. Spira
Keyword(s):  
Serum Proteins ◽  
Disc Electrophoresis ◽  
Normal Serum

Agammaglobulinemia, by Col. Ogden C. Bruton, MC, USA,Pediatrics, 1952;9:722–728

PEDIATRICS ◽  
1998 ◽  
Vol 102 (Supplement_1) ◽  
pp. 213-215
Author(s):  
Rebecca H. Buckley
Keyword(s):  
Gamma Globulin ◽  
Serum Proteins ◽  
Good Health ◽  
Electrophoretic Analysis ◽  
Functional Change ◽  
Extensive Study ◽  
Normal Serum ◽  
Dramatic Improvement ◽  
Serum Globulin ◽  
Pneumococcal Sepsis

A hitherto unrecognized entity manifested by complete absence of gamma globulin with otherwise normal serum proteins and recurrent pneumococcal sepsis is described in an 8-year-old male. The patient appeared to be normal in other respects and, after extensive study, no structural or functional change could be demonstrated in any body system. He was unable to produce antibody to the pneumococcus with the four antigenic substances used; a positive Schick test persisted despite numerous attempts to reverse it with diphtheria toxoid. No antibody could be demonstrated following administration of typhoid vaccine in the usual manner, and his serum was negative for complement-fixing antibodies of epidemic parotitis after he experienced a typical clinical picture of that disease. Gamma globulin could be demonstrated in his serum after concentrated immune human serum globulin was administered subcutaneously, and its gradual disappearance could be followed by electrophoretic analysis over a period of approximately six weeks. Concurrently, and following administration of human gamma globulin (3.2 gm. gamma globulin) at monthly intervals, he had been free of pneumococcal sepsis for more than a year, whereas he had experienced clinical sepsis at least 19 times in the previous four years. Eight different types of pneumococci had been recovered from blood cultures during 10 different episodes of sepsis. In the Discussion, [the author] concluded that there was a cause-and-effect relationship between the absence of gamma globulin and the repeated infections, based on the child's dramatic improvement after beginning gamma globulin therapy. [The author] proposed two possible causes–congenital or acquired. While [he] felt that the patient's good health for the first 4.5 years of life argued against a congenital cause, the persistence of the defect supported it.

scholarly journals THE OCCURRENCE DURING ACUTE INFECTIONS OF A PROTEIN NOT NORMALLY PRESENT IN THE BLOOD

1947 ◽  
Vol 85 (5) ◽  
pp. 491-498 ◽  
Author(s):  
Maclyn McCarty
Keyword(s):  
Infectious Diseases ◽  
Early Phase ◽  
Serum Proteins ◽  
Protein A ◽  
Normal Serum ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Acute Infections

A procedure is described for the isolation and crystallization from human serous fluids of the C-reactive protein, a substance which appears in the blood especially in the early phase of certain acute infectious diseases. Immunological studies confirm earlier work in showing that the protein is highly antigenic and serologically specific, and demonstrate that crystallization of the protein effectively separates it from normal serum proteins.

scholarly journals Capacity of human serum to depolymerize actin filaments

Blood ◽  
1987 ◽  
Vol 70 (2) ◽  
pp. 524-530
Author(s):  
PA Janmey ◽  
SE Lind
Keyword(s):  
Human Serum ◽  
Actin Filaments ◽  
Serum Proteins ◽  
Normal Serum ◽  
Slow Phase ◽  
Rapid Phase ◽  
Plasma Gelsolin ◽  
Preferential Formation

Human blood depolymerizes filamentous (F-)actin. The interaction of actin filaments and monomers with human serum was studied by following the kinetics and extent of the depolymerization of pyrene-labeled F- actin and by analysis of serum proteins adhering to immobilized actin monomers. In physiologic Ca2+ concentrations, the depolymerization of F- actin proceeds in two stages: a rapid phase, attributed to direct severing of filaments by plasma gelsolin, and a slow phase attributed to the binding of actin monomers to vitamin D-binding protein (DBP). Without Ca2+, only the slow phase is observed. Human serum can completely depolymerize 10 to 18 mumol/L of actin, of which approximately 5 mumol/L occurs rapidly. Depolymerization can be accounted for by the normal serum concentrations of gelsolin and DBP. Fibrin(ogen) and fibronectin, which bind actin in vitro, do not contribute to the kinetics or extent of its depolymerization. Affinity chromatography and functional assays for the presence of gelsolin-actin complexes show that addition of G-actin to serum results in preferential formation of actin-DBP complexes, but that addition of F- actin to serum produces both gelsolin-actin complexes and DBP-actin complexes. The distinctive binding of actin monomers and polymers to these two serum proteins suggests a means by which their coordinated actions are maximized in vivo, from the standpoint of depolymerizing filaments and clearing monomers from the circulation.

Effects of streptozotocin-induced diabetes on rough endoplasmic reticulum and lysosomes of rat liver

1992 ◽  
Vol 263 (5) ◽  
pp. E856-E862
Author(s):  
S. E. Lenk ◽  
D. Bhat ◽  
W. Blakeney ◽  
W. A. Dunn
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Serum Proteins ◽  
Serum Insulin ◽  
Normal Serum ◽  
Lysosomal Hydrolases ◽  
Insulin Dependent ◽  
Streptozotocin Induced Diabetes ◽  
Endogenous Proteins ◽  
Vacuolar System

In the absence of amino acids and insulin, ribosome-free regions of the rough endoplasmic reticulum (RER) invaginate to form an autophagosome, which matures into an autolysosome (W. A. Dunn, Jr., J. Cell Biol. 110: 1923-1933, 1990). In this study, biochemical and morphological methods were used to examine the structure and integrity of the RER and the lysosome-vacuolar system in livers of untreated (normal serum insulin) and streptozotocin (STZ)-treated (depressed serum insulin) fed and fasted rats. Degradation of endogenous proteins was increased by 70% in STZ-treated animals. Proteolysis was further enhanced when these animals were deprived of food for 24 h. These alterations in protein turnover were accompanied by increases in the fractional volume of autophagic vacuoles and in the hepatic amounts of three lysosomal hydrolases. These effects of STZ were prevented on administration of insulin. In addition, there was an insulin-dependent 50% loss of RER surface area in livers from STZ-treated rats. This loss of structural RER was accompanied by comparable decreases in the cellular amounts of two RER membrane proteins and one luminal protein, suggesting that the RER was degraded as a unit. Additional losses of RER were observed when STZ-treated rats were fasted. Furthermore, the hepatic amounts of two serum proteins decreased, suggesting the functional capacity of the RER was reduced. Combined, the data suggest that in STZ-induced diabetes the losses in RER are related to enhanced autophagy.

Binding of labeled thyroxin analog to serum proteins evaluated after radioimmunoassay of free thyroxin.

1989 ◽  
Vol 35 (3) ◽  
pp. 475-477 ◽  
Author(s):  
G Arevalo
Keyword(s):  
Serum Proteins ◽  
Equilibrium Dialysis ◽  
Normal Serum ◽  
Thyroid Status ◽  
Nonthyroidal Illness ◽  
Serum Pool ◽  
Normal Individuals ◽  
Ambulatory Patients ◽  
One Step

Abstract In ambulatory patients, assay of free thyroxin (FT4) in serum correlates well with thyroid status and with results obtained by equilibrium dialysis. The validity of FT4 results has been questioned mainly in euthyroid patients with altered concentrations of thyroid hormone-binding proteins, as in nonthyroidal illness, hereditary analbuminemia, familial dysalbuminemic hyperthyroxinemia (FDH), and the presence of iodothyronine-binding antibodies. I present here a study of the binding of [125I]T4-derivative to serum proteins in the supernate, which is ordinarily discarded after determination of FT4 by one-step radioimmunoassay with dextran-coated charcoal used to separate the free and bound fractions. The results are expressed as a ratio, with results for a normal serum pool as reference. The average ratio was high in hyperthyroid subjects, 1.26 (SD 0.12, n = 25), and in hypoalbuminemia, 1.20 (SD 0.10, n = 15), and low in FDH, 0.62 (SD 0.11, n = 9), and hypothyroid subjects, 0.90 (SD 0.06, n = 20). In normal individuals it was 0.98 (SD 0.05, n = 30). Determination of the analog-binding rate complements the FT4 result and allows for the recognition of cases with abnormal binding by serum proteins, without recourse to other tests recommended for thyroid-function studies.

scholarly journals Immunohistochemical study of the blood-brain barrier. Production of an artifact.

1980 ◽  
Vol 28 (6) ◽  
pp. 570-572 ◽  
Author(s):  
J R Sparrow
Keyword(s):  
Central Nervous System ◽  
Blood Vessels ◽  
Serum Proteins ◽  
Immunohistochemical Study ◽  
Normal Serum ◽  
Frozen Sections ◽  
Immunohistochemical Technique ◽  
The Central Nervous System ◽  
Cryostat Sections ◽  
The Brain

The permeability to normal serum proteins of blood vessels in the central nervous system (CNS) was studied by means of the peroxidase-antiperoxidase immunohistochemical technique. Frozen sections were cut in a cryostat and then fixed briefly in 95% ethanol. The localization of serum proteins outside blood vessels in the brain was shown to be an artifact produced during the preparation of cryostat sections. It was concluded that such cryostat sections are unsuitable for studies of vascular permeability in the CNS.

The Development of a Radioimmunoassay Procedure for the Estimation of Tamm—Horsfall Glycoprotein in Human Serum

1977 ◽  
Vol 52 (2) ◽  
pp. 183-191 ◽  
Author(s):  
P. J. G. Avis
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Solid Phase ◽  
Normal Serum ◽  
Small Sample ◽  
Agarose Beads ◽  
Assay Procedure ◽  
Series Of Experiments ◽  
Sepharose 4B ◽  
Cyanogen Bromide Activation

1. A quantitative radioimmunoassay was developed for the measurement of nanogram amounts of Tamm—Horsfall (TH) glycoprotein in the presence of serum proteins at concentrations above 30 mg/ml. 2. Specific anti-(TH-glycoprotein) antibodies were labelled with 125I and these were usable for a period of 8 weeks. 3. Agarose beads (Sepharose 4B), to which TH-glycoprotein had been coupled via cyanogen bromide activation of the Sepharose, were used as the solid phase in the assay. This proved stable upon storage at 4°C for periods in excess of 4 months. 4. The dissociation of the glycoprotein in the presence of serum proteins that was necessary for quantification was achieved by subjecting the sample to ultrasonication. 5. Assays conducted on a small sample of normal serum produced evidence that normal serum contained amounts (50–180 ng/ml) of a substance that reacted similarly to TH-glycoprotein in the assay procedure and in a series of experiments conducted to confirm the presence of this substance in human serum.

Evidence for an inhibitor of renal urate and PAH secretion in rabbit blood

1983 ◽  
Vol 244 (6) ◽  
pp. F590-F598
Author(s):  
R. J. Tanner ◽  
A. M. Chonko ◽  
R. M. Edwards ◽  
J. J. Grantham
Keyword(s):  
Serum Proteins ◽  
Organic Anion ◽  
Synthetic Medium ◽  
Normal Serum ◽  
Rabbit Serum ◽  
Tetraethylammonium Bromide ◽  
Transport Inhibitor ◽  
Urate Transport ◽  
Allosteric Modification ◽  
Urate Secretion

Results of previous studies of urate secretion in isolated perfused S2 segments of the rabbit proximal tubule suggested that a bath of rabbit serum may inhibit urate transport in comparison to a synthetic medium. In the current study we tested for a urate transport inhibitor by determining the steady-state tissue-to-medium ratio (T/M) of [14C]urate in nonperfused S2 segments during incubation in synthetic medium (BSA-Burg) and commercial rabbit serum (RS-PF). With 80-120 microM urate in the bath the T/M ratio was 7.66 +/- 0.53 (n = 29) in BSA-Burg and 5.29 +/- 0.40 (n = 29) in RS-PF. RS-PF decreased the influx of urate into the cells but had no effect on urate efflux. Freshly drawn rabbit serum and plasma also inhibited urate accumulation, and the inhibition was reversible. p-Aminohippurate accumulation was inhibited by RS-PF, but tetraethylammonium bromide uptake was not. RS-PF inhibited transepithelial secretion of urate and PAH, but net fluid absorption was not decreased. The inhibitory material in rabbit serum could not be removed by extensive dialysis (14,000-dalton exclusion), by ultrafiltration (50,000-dalton exclusion), or by charcoal or ethanol extraction. Inhibitory activity was detected in both albumin and globulin fractions of rabbit serum. The relation between bath and intracellular urate concentrations of nonperfused tubules in rabbit serum was sigmoidal, whereas the relation in the BSA-Burg medium was more nearly hyperbolic. We conclude that organic anion transport in rabbit S2 segments is inhibited or suppressed by normal serum and suggest that urate secretion and excretion may be subject to allosteric modification by serum proteins.

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