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PubMed1987

[Interaction of sheep haptoglobin with trypsin inhibitors].

It was found that polymeric sheep haptoglobin C interacts with duck egg ovomucoid and with maize trypsin inhibitor. These inhibitors do not block the region in haptoglobin C molecule which is responsible for the formation of its complex with hemoglobin. The binding of the natural protein inhibitors is suggestive of homology of the haptoglobin site involved in the interaction with the substrate-specific site of trypsin. It is assumed that the regions in these protein molecules adjacent to the active and specific sites also possess a high degree of homology.

Animals↗
PubMed1988

[Investigation of the distribution of haptoglobin genotypes in human populations].

Distribution of haptoglobin genotypes in a number of population specimens of the main World regions is studied. New statistics permitting to reveal deviation from the Hardy - Weinberg equilibrium and its direction (towards either deficiency or excess of heterozygotes) are proposed. S-statistics, based on the model of selection against homozygotes, can be used for quantitative estimation of the deviation. In this way, statistically significant excess of heterozygotes was found in European, North Asia and North American populations. In some areas, the coefficient of selection (S-statistics) is about 10%. Additional data which reflect different adaptive values of haptoglobin genotypes permit to suppose that the existence of haptoglobin polymorphism is provided by both higher fertility and lower viability of homozygotes Hp 2-2.

Asia↗
PubMed1987

Factors influencing the reaction of haptoglobin with concanavalin A in affino-immunoelectrophoresis.

In crossed affino-immunoelectrophoresis pure haptoglobin or that present in serum moved in the shape of either non-retarded or weakly-, or strongly-retarded fractions, related to varying Con A concentrations included into the first dimension gel. At low concentrations of Con A non-, weakly-, and strongly-retarded fractions were observed, whereas at higher concentrations only one, strongly-retarded fraction could be found. The number and percentage composition of haptoglobin fractions were dependent not only on the concentration of Con A, but also on other proteins added to the sample submitted to electrophoresis. Irregular distribution of haptoglobin Con A-dependent fractions made quantitative measurements unreliable.

Concanavalin A↗
PubMed1986

Haptoglobin type and liver disease.

The haptoglobin phenotype has been estimated in patients suffering from chronic liver disease (n = 222) and acute hepatitis (n = 59) in comparison with the haptoglobin pattern of a normal population (n = 1726). The frequency of Hp 1-1 was significantly increased in non-alcoholic chronic liver disease (p = 5%; chi 2-test) in contrast to alcoholic disease. The highest incidence of Hp 1-1 occurred in cryptogenic cases (p = 1%). The follow-up of patients suffering from acute hepatitis failed to indicate any relationship between the haptoglobin phenotype and the course of hepatitis. The results suggest that Hp 1-1 is a genetic marker of special kinds of chronic liver diseases.

Acute Disease↗
PubMed1985

Discontinuous polyacrylamide gel electrophoresis for typing haptoglobin in bloodstains.

A routine method is described for obtaining reproducible haptoglobin patterns from bloodstains by discontinuous polyacrylamide gel electrophoresis. By employing a stacking gel, proteins from bloodstain extracts are concentrated into narrow zones, before entering the resolving gel. This effect yields highly resolved haptoglobin patterns. Therefore, laboratories without the specialized equipment and expertise for polyacrylamide gradient gel preparation can still obtain highly resolved haptoglobin patterns from bloodstains.

Blood Grouping and Crossmatching↗
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↗
PubMed1980

[Peroxidase properties of sheep haptoglobin complexes with hemoglobins of various types of animals].

It was found that haptoglobins from adult sheep and sheep foetus form active saturated complexes with sheep, cow, horse, mouse and human haemoglobins and with sheep foetus haemoglobin. This suggests that haemoglobin binding to haptoglobin does not depend on the species. The increase in the peroxidase activity during complex formation occurs in case of all haemoglobins; however, the degree of this increase is variable. This is probably due to the fact that during complex formation the haemoglobin molecule is stabilized, but no activation of Hb occurs. It can be assumed that the sites of the haptoglobin and haemoglobin molecules responsible for complex formation are relatively conservative in the course of evolution because of the physiological significance of the complex formation reaction.

Animals↗
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↗
PubMed1982

[Haptoglobins, streptococcus agglutination and streptococcal infections].

The haptoglobins in man and in mammals react with streptococci bearing the T4-antigen. Hp 2-2 and Hp 2-1 react with high titres like complete agglutinins while Hp 1-1 acts like a blocking antibody. It is surprising to observe the similarity of the behaviour of the haptoglobins and of IgG and IgM. Streptococci carrying Hp 1-1 yield a positive Coombs-test. The Coombs-serum however, is an anti-human-haptoglobin-body from sheep. By means of supplements it has been possible to increase partly considerably the titres of Hp 2-1 and Hp 2-2 against the streptococci.

Agglutination↗
PubMed1983

Intermediates in the reassociation of reduced haptoglobin.

Oxidative reassociation of alpha and beta subunits of human and equine haptoglobins as well as of two 2 alpha . 2 beta tetrameric hybrids made of subunits of each haptoglobin was studied following reduction of interchain disulphide bridges and also with isolated, PHMB-protected subunits in homologous and heterologous systems. Molecular mass and subunit composition of the intermediates appearing in the process of successive oxidation of -SH groups were determined by SDS-polyacrylamide-gel electrophoresis. The yield of subunit reassociation into homologous and heterologous tetramers 2 alpha . 2 beta was very high (75-80%) and the reassociated haptoglobins exhibited properties of native proteins in binding reactions with haemoglobin and with specific antibodies.

Animals↗
PubMed1982

Serum haptoglobin: a nonspecific tumor marker for renal cell carcinoma.

Serum haptoglobin levels were measured in 116 patients with renal cell carcinoma. The overall accuracy of correlation between haptoglobin levels and the presence or absence of known disease was 68% (normal in 87% of patients without clinically apparent disease, and elevated in 58% of patients with disease). The levels appear to correlate with the extent of tumor burden: stable when clinical disease is stable, rising as disease progresses, and falling after effective therapy. Serum haptoglobin is rarely falsely elevated, which suggests an excellent potential for disease surveillance. This nonspecific tumor marker appears to merit further evaluation in patients with renal cell carcinoma.

Adenocarcinoma↗
PubMed1981

Study of hemoglobin synthesis by affinity chromatography on Sepharose haptoglobin.

An affinity chromatography system, using haptoglobin bound covalently to Sepharose 4B, has been developed to purify human hemoglobin from soluble non-heme proteins. Agarose-haptoglobin specifically binds hemoglobin. Globin chains were eluted from the agarose-haptoglobin after removal of the heme. This method has allowed accurate measurements of globin chain synthesis in blood and bone marrow samples from adults and in culture of early erythroid precursors present in adult blood or bone marrow.

Bone Marrow↗
PubMed1995

[Serum levels of IgG, IgA, IgM, transferrin and haptoglobin. III. Results obtained with monoclonal immunoglobulins].

This study is the third part of a multicenter evaluation carried out with ten analysers. Five proteins (IgG, IgA, IgM, transferrin, haptoglobin) were assayed in three sera, each containing one monoclonal Ig (IgG, IgA, or IgM). The expected agreement was not obtained with these particular sera, except in the case of haptoglobin. The marked imprecision of the monoclonal Ig quantification is highlighted, including the fact that many erroneous results are due to the antigen excess phenomenon. It is also shown that in the serum containing monoclonal IgM, quantification of the other proteins, remaining polyclonal Ig, as well as transferrin and haptoglobin, is difficult. The authors recall that electrophoresis and immunoelectrophoresis, which are indispensable for the characterization of the monoclonal components, are of great help in solving such difficulties.

Blood Chemical Analysis↗
PubMed1993

The molecular weights of twelve apolipoprotein(a) variants, determined using haptoglobin 2-2 polymer molecular weight standards.

Apolipoprotein(a) [apo(a)] variants were characterized in 398 sera by immunoblotting: (a) by molecular weight, using a haptoglobin 2-2 polymeric series as standards, and (b) by nomenclature, using serum pools containing previously characterized apo(a) variants as standards. The haptoglobin 2-2 standard curve (172-859 kDa) alleviates the necessity of obtaining molecular weights by extrapolation. Among the 398 sera, 40.2% had double apo(a) bands (54 phenotypes), 58.0% had a single apo(a) band and 1.8% were null (no bands observed). An inverse, though non-monotonic, relationship was observed between apolipoprotein(a) molecular weight and serum lipoprotein(a) [Lp(a)] concentration. Due to the large size of apo(a) and the relatively small increment between variants (15-16 kDa), molecular weight could not be used alone to characterize variants. Even with a CV of 3-4%, there was an overlap between variant molecular weight estimates. However, in combination with the identification of variants by comparison with standards, the haptoglobin 2-2 standard curve could be used to obtain mean molecular weight estimates for each variant. 12 distinct variants were identified among the sera, with apparent mean molecular weights of 314, 388, 410, 433, 454, 466, 503, 519, 528, 543, 553 and 572 kDa, respectively. These molecular weight estimates are consistent with the theoretical molecular weight range for apo(a) variants, calculated from sequence and carbohydrate analysis, of 238-643 kDa.

Apolipoproteins A↗
PubMedDate not supplied

[Serum haptoglobin in lung cancer patients].

Changes in the concentration of haptoglobin-glycoprotein-globulin fraction of blood serum were studied in patients with lung cancer. It was found, that haptoglobin concentration increased in accordance to a disease stage. Formation of haptoglobin hemoglobin (Hp-Hb) complex in the sera of patients may be of great importance for neutralization of superoxidative products.

Blood Donors↗