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PubMedDate not supplied

[Effect of ACTH on the excretion of acid glycosaminoglycans in urine and on the content of haptoglobin in blood serum of rats in acute aseptic inflammation].

In aseptic inflammation an increase in excretion of acid glucosoaminoglycans with urine of rats was an earlier evidence for destructive processes in the main substance of connective tissues than an increase in content of haptoglobin in blood serum. The increase in content of haptoglobin in blood serum was probably caused by beginning reparative processes in the centre of impairment. The centre of inflammation, caused by subcutaneous administration of turpentine simultaneously with repeated injections of high doses of ACTH, was maintained in the rats longer than in animals, which were not treated with ACTH. In the case the most distinct increase in excretion of glycosoaminoglycans with urine was observed; content of haptoglobin was also increased in blood serum.

Acute Disease↗
PubMed1978

[Haptoglobins in gynecologic tumors (author's transl)].

Serum concentrations of haptoglobins were checked in 100 women with benign or malign gynecologic tumors. Typification of haptoglobins was determined by starch gel electrophoresis, quantification by single radial immunodiffusion. Cases with malignancies showed significant increased levels in comparison to healthy women. In cases with cervical carcinoma, a significant increase of the haptoglobin level was evaluated according to advanced carcinoma.

Electrophoresis, Starch Gel↗
PubMed1979

[Simple method for the preparation of haptoglobin].

The present paper deals with a method permitting the isolation of haptoglobin 2-2 from human serum or plasma. The haptoglobin is adsorbed to DEAE-cellulose at pH 5.1 by batching. The loaded cellulose is given into a column and the haptoglobin eluted by a 0.1 M to 0.15 M acetate buffer. The last step is a gel-chromatography on Sephadex G-200. Disc- and immunoelectrophoresis were used to test the purity. As by-product acid alpha1-glycoprotein can be obtained.

Blood Proteins↗
PubMed1979

Significance of serum fucose, sialic acid, haptoglobine and phospholipids levels in the evolution and treatment of breast cancer.

Serum fucose, sialic acid, haptoglobine and phospholipids were determined in 167 women with breast cancer stages I--III, 30 with benign lesions of the breast, 42 women in various physiological states of the mammary gland (pregnancy, early childbed and lactation) and compared with 30 healthy women as control. Serial determinations of these parameters during the radio-surgical treatment were done in 28 patients with breast cancer stage III. Fucose and phospholipids levels were significantly increased respectively decreased in the group of patients with breast cancers but unmodified in the others. Sialic acid and haptoglobine -- increased in patients with cancer -- were also elevated in patients with early childbed and benign affections of the breast. The surveillance of these four parameters during the radio-surgical treatment of breast cancer evidenced a good correlation between their modified levels and clinical state of the patients. The increase in fucose, sialic acid and haptoglobine respectively the decrease in phospholipids levels was associated with the clinical evidence of recurrences and metastases.

Breast Diseases↗
PubMed1979

An efficient method to eliminate streaking in the electrophoretic analysis of haptoglobin in bloodstains.

A bloodstain extraction procedure that improves the analysis of haptoglobin in dried bloodstains has been developed. The streaking of electrophoresis gels caused by deteriorated hemoglobin can be eliminated by incorporating chloroform in the bloodstain extraction procedure. The method is easier to execute than previously published techniques for eliminating the adverse effects of deteriorated hemoglobin on the analysis of haptoglobin. Bloodstains up to two years old were correctly phenotyped in haptoglobin by this method.

Blood Group Antigens↗
PubMed1978

Degradation and inactivation of ceruloplasmin and haptoglobin by rat liver lysosomes and some other proteinases.

Lysosomal fraction was isolated from rat liver by density gradient centrifugation after pervious loading of lysosomes in vivo with Triton WR-1339. Tritosome preparations were incubated at 37 degrees C and pH 5 for 24 hr with purified human ceruloplasmin or haptoglobin. After this period approximately 20% of total alpha amino nitrogen was released from ceruloplasmin and over 40% from haptoglobin. This was accompanied by loss of peroxidase activity of haptoglobin (in complex with haemoglobin), while enzymatic activity of ceruloplasmin remained unaltered. Removal of sialic acid by neuraminidase had no effect on digestion of ceruloplasmin by rat liver tritosomes. Both glycoproteins were resistant to horse leucocyte proteinases and pancreatic eleastase but were easily inactivated by trypsin and chymotrypsin.

Animals↗
PubMed1977

The frequency in Japanese of genetic variants of 22 proteins. I. Albumin, ceruloplasmin, haptoglobin, and transferrin.

This paper presents the results of an electrophoretic survey of approximately 4000 individuals from the cities of Hiroshima and Nagasaki, Japan, for four serum proteins: albumin, ceruloplasmin, haptoglobin and transferrin. The haptoglobin gene frequencies obtained for the HP1-HP2 polymorphism are in agreement with earlier reports. Rare electrophoretic variants of albumin, ceruloplasmin and haptoglobin occur with frequencies of 2-48, 0-50 and 0-58 per 1000 determinations, respectively. The noteworthy finding of 8 distinct transferrin variants in these populations, with a combined frequency of 20-90 per 1000 determinations, is also presented. Four of these variants (Dchi, B1, B3, and DHIR2 which corresponds electrophoretically to D4) have been reported in other populations in Japan, but the other five have not previously been differentiated.

Blood Protein Electrophoresis↗
PubMedDate not supplied

[Haptoglobin and ceruloplasmin in systemic scleroderma].

Content of haptoglobin and ceruloplasmin was estimated in blood serum of 23 patients with sclerodermia systematica. A statistically distinct decrease in ceruloplasmin concentration was observed in blood of the patients, whereas content of haptoglobin was markedly increased; this phenomenon reflects a level of the pathological process activity. The proteins are synthesized in various zones of liver lobes: haptoglobin--in the central zone, ceruloplasmin - in the peripheral one. Decrease in content of ceruloplasmin in blood of patients with sclerodermia systematica was due to impairment of hepatocytes, localized in peripheral parts of liver lobes.

Animals↗
PubMed1979

Effects of bacterial endotoxin and corticosteroids on plasma concentrations of alpha 2 macroglobulin, haptoglobin and fibrinogen in rats.

Bacterial endotoxin injected into rats resulted in increased plasma concentration of alpha 2 macroglobulin, haptoglobin and fibrinogen. Cortisone acetate injected i.m. by itself was sufficient to increase the plasma concentration of haptoglobin by 54% and to a lesser extent the concentrations of the other two proteins. When cortisone acetate and/or cortisol succinate were injected simultaneously with varying doses of endotoxin, the effects of the corticosteroid differed for each plasma protein. Doubtless because of the effect of cortisone by itself the slope of the dose-response relationship for haptoglobin was greatly reduced. In contrast to this the slope for alpha 2 macroglobulin was reduced and that for fibrinogen was unaffected. These findings suggest that, if effects due to endogenous corticosteroids are to be avoided, increases in plasma fibrinogen will serve best as indicators of stimulation of the acute-phase response. Since, however, the relative increase of alpha 2 macroglobulin due to the lowest dose of endotoxin was much greater than that of fibrinogen, increases in concentration of the former protein represent the most sensitive indication of the acute-phase response. Consideration of the responses in individual rats has made possible division into those with more or less than average increases for all 3 plasma proteins and those showing irregular responses. Especially in the group which had received the lowest dose of endotoxin, a much larger number than would be expected on a random basis was found to respond regularly with either more or less than average increases for all 3 proteins.

Animals↗
PubMed1976

Diagnostic value of ceruloplasmin, haptoglobin and sialic acid in chronic pyelonephritis.

In a group of 84 patients with exacerbated chronic pyelonephritis the authors have determined the blood serum levels of ceruloplasmin, haptoglobin and sialic acid before, during and after antibacterial treatment. They have found a decrease in these levels following treatment. The results of ceruloplasmin, haptoglobin and sialic acid assays could be used as an index for the activity of the pathologic process, as well as in the differential diagnosis between pyelonephritis and glomerulonephritis.

Ceruloplasmin↗
PubMed1977

Immunochemical comparison of human and goat haptoglobin and alpha 2-macroglobulin.

1. A non-haptoglobin alpha 2-globulin was observed in the plasma of goats (Capra hircus) after inflammatory stresses. 2. This stress reaction protein exhibited an electrophoretic mobility and molecular weight similar to goat haptoglobin. 3. Complete immunological cross-reactivity was demonstrated between the goat protein and human alpha 2-macroglobulin. 4. The functional and evolutionary significance of these observations are discussed.

Animals↗
PubMed1978

Acute phase reactants ceruloplasmin and haptoglobin and their relationship to plasma prostaglandins in rabbits bearing the VS2 carcinoma.

Results of previous studies have shown that the VX2 carcinoma in rabbits synthesizes large amounts of prostaglandin E2 (PGE2). PGE2 secreted by the tumor is rapidly metabolized and can be measured in plasma as the metabolite 13,14-dihydro-15-keto-PGE2 (PGE2-M). We have previously proposed that the hypercalcemia that occurs in rabbits bearing the VX2 carcinoma is due to excessive secretion of PGE2 by the tumor and its subsequent action on the skeleton as a bone resorption-stimulating factor. In the course of these studies, we noted that the plasma of rabbits bearing the VS2 carcinoma became blue about 1 wk after tumor implantation. The intensity of the color increased markedly thereafter. We therefore measured ceruloplasmin in plasma by both chemical and immunological assay methods. Plasma ceruloplasmin and PGE2-M rose in parallel (within 7-10 days) and preceded by 7-10 days the development of hypercalcemia. 2 wk after tumor implantation, plasma PGE2-M and ceruloplasmin had risen about 20- and 6-fold, respectively, while the rise in plasma calcium was just beginning. Indomethacin, an inhibitor of prostaglandin synthesis, given from the time of tumor implantation prevented completely the hypercalcemia and largely inhibited the rise in ceruloplasmin. When given after hyperprostaglandinemia had developed, indomethacin produced a fall in both PGE2-M and ceruloplasmin. A rise in plasma haptoglobin concentrations similar to that seen for ceruloplasmin was also observed. No changes in plasma albumin concentrations occurred. We conclude that the acute phase reactants ceruloplasmin and haptoglobin rise rapidly in the plasma of rabbits bearing the VX2 carcinoma, and that this increase is related to arachidonic acid metabolism in these animals. It is possible that arachidonic acid metabolites also play a role in the elevations of these two plasma proteins observed in certain patients with malignant tumors.

Animals↗
PubMed1975

Proteolytic degradation of hemoglobin-haptoglobin complex by lysosomal enzymes from rat liver.

The catabolic degradation of hemoglobin and of its complex with haptoglobin by lysosomal enzymes from rat liver was studied with special emphasis on the action of cathepsins D and E. The digestion of free hemoglobin can be mainly attributed to the action of cathepsin D [EC 3.4.23.5], while the digestion of the complex in the pH rand 2-3 is due more to the action of cathepsin E than that of cathepsin D. The enzymic activities of both cathepsins were strongly inhibited by pepstatin, and 4M urea inactivated cathepsin E. Measurements of the peroxidase activity and optical rotatory dispersion of the hemoglobin-haptoglobin complex showed that the complex suffered rapid denaturation below pH 2.9.

Animals↗
PubMed1975

C3, GBG, orosomucoid and haptoglobin polymorphisms. Improved staining methods.

C3, GBG, and orosomucoid polymorphisms were electrophoresed in a high-voltage agarose method which permitted the typing of 15-20 samples. The increased sensitivity of the dye Coommassie blue was used to stain the protein, and yielded higher resolution than amido black. The typing of haptoglobin samples, was facilitated by devising a method which utilizes the peroxidase activity of the haptoglobin-hemoglobin complex with 90-tolidine and hydrogen peroxide as substrates and 4-chloro-1-naphthol as coupler.

Complement System Proteins↗
PubMed1976

The purification of porcine haptoglobin by affinity chromatography with concanavalin A-Sepharose.

Methods designed for the isolation of human haptoglobin (Hp) were found insufficient when applied to pig plasma due to the formation of a material tentatively identified as albumin dimer. Small scale separation is possible by preparative polyacrylamide gel electrophoresis. Larger scale purification from nonglycoprotein contaminants such as albumin dimer is achieved by affinity chromatography using immobilized concanavalin A. Porcine haptoglobin is microheterogeneous. More than 14 components, partially resolveable by gel filtration, were detected.

Animals↗
PubMed1976

The reaction between hemoglobin alpha-subunit and haptoglobin.

The interaction between human hemoglobin alpha-subunit and porcine haptoglobin was investigated by polyacrylamide gel electrophoresis, gel filtration chromatography, sedimentation through excess alpha-subunit and gel filtration in an alpha-subunit-containing medium. No interaction was detected by the first two methods indicating dissociation of the complex during the application of these separation techniques. The latter two methods, in which the complex is studied in a medium of excess subunits, showed that haptoglobin became saturated with the binding of two alpha-subunits.

Animals↗
PubMed1976

[Usual values of haptoglobin, protein-bound sialic acid and blood sedimentation in a population of the Cherbourg region].

The authors studied 3 parameters commonly used for the exploration of an inflammatory syndrome (determination of globular sedimentation rate at the first and second hour, concentration of plasma haptoglobin, sialic acid bound to plasma proteins rate). Haptoglobin and acid sialic assays were solely used in determining a control population (816 patients without any inflammatory reaction). As a matter of fact, the values we found complied with a normal distribution rule and confidence limits with a probability of 95% were obtained.

Blood Sedimentation↗
PubMed1976

Different susceptibilities to intracellular proteases of hemoglobin and hemoglobin-haptoglobin complex.

The susceptibilities of hemoglobin and hemoglobin-haptoglobin complex to intracellular proteases differ significantly. Hemoglobin and hemoglobin-haptoglobin complex are degested in the regions of pH 5.5-2.5 and 4.0-2.5 respectively, having pH optima at pH 4.0 and 3.0 respectively, by intracellular proteases from rat and mouse liver or spleen. The difference in proteolytic susceptibility is found to be due to the different stabilities to acid among hemoglobin derivatives as evidenced by the measurements of their helical contents in acidic pH.

Animals↗