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Biomedical subjects

H Haupt

Publications and source records attributed to H Haupt.

At least 127 records · Page 7Linked to original sources
PubMed1977

[Isolation and characterization of 7S-beta1-globuline from human erythrocytes (author's transl)].

A new protein was isolated from lysates of washed human erythrocytes in a two step procedure using ionexchange chromatography and gel filtration. The protein has the electrophoretic mobility of a beta1-globulin. On ultracentrifugation the purified protein when dissolved in a 0.05 M phosphate buffer (pH 6.8), containing 0.2 M NaCl sediments with 6.88 S and shows a molecular weight of 150,000-180,000 daltons. In salt solutions with higher ionic strength the molecules dissociate reversibly into subunits which have a molecular weight of 40,000-45,000 daltons. The 7S-beta1-erythrocyte protein according to its behavior at ultracentrifugation, gel filtration and SDS poly-acrylamide gel electrophreses apparently is composed of 4 identical or similar subunits which are loosely held together by noncovalent bonds. Chemically the 7S-beta1-erythrocyte protein consists of 99% amino acids and 1% carbohydrates. The concentration of this protein in erythrocytes amounts to 250 mg per 100 ml packed red blood cells. The protein is not found in the membrane. In its physical, chemical and immunochemical properties the 7S-beta1-erythrocyte protein differs from all other well defined proteins and enzymes from human red cells thus far known.

Beta-Globulins↗
PubMed1977

[Serum cholinesterase as a model glycoprotein (author's transl)].

Human serum cholinesterase (EC 3.1.1.8) is a carbohydrate-rich glycoprotein, which reacts with 18 different lectins from plants and invertebrates by a specific precipitin reaction; most of the lectins combine with alkali-stable bound carbohydrate chains. One third of these lectin receptors appear after neuraminidase-treatment, two thirds can be demonstrated before and after removal of neuraminic acid. The specific lectin receptors of the alkali-labile carbohydrate chains are characterized and analyzed by chemical and serological methods.

Agglutinins↗
PubMed1977

[Isolation and characterization of an unknown, leucine-rich 3.1-S-alpha2-glycoprotein from human serum (author's transl)].

This article describes the isolation and characterization of a previously unknown, leucine-rich 3.1S-alpha2-glycoprotein from human serum. The starting material was Supernatant II, which is a byproduct in the large-scale preparation of albumin and gamma-globulin by the ethacridine lactate/ammonium sulfate procedure. The purified protein is homogenous both in carrier-free and molecular-sieve electrophoresis. Its electrophoretic mobility indicates that it belongs to the alpha2-globulins. Isoelectric focussing splits it into 4 bands with isoelectric points between 3.8 and 4.1. In the ultracentrifuge it sediments in a single band at 3.1S. The molecular weight determined by equilibrium sedimentation is 49 600 +/- 4 000. Subunits were not detected. Chemical analysis reveals it to be a glycoprotein with a carbohydrate content of 23%. The amino acid content is unusual in that the leucine content is almost 17%, i.e. about every fifth amino acid is a leucine. The average concentration of the leucine-rich 3.1S-alpha2-glycoprotein in human serum was determined by a quantitative immunological method as 2.1 mg per 100 ml. The protein is not related to any of the previously known well characterized serum proteins.

Alpha-Globulins↗
PubMed1976

[Comparative studies of lactate concentration in the perilymph, blood and cerebrospinal fluid of normal and sound exposed guinea pigs (author's transl)].

The paper deals with comparative studies of lactate concentration in the perilymph (PL) of scala tympani and of scala vestibuli, arterial and venous blood, serum and cerebrospinal fluid (CSF) of normal and sound exposed guinea pigs, special consideration having been given to possible sources of error in the methods employed. Lactate was determined enzymatically using a micromodification of the Boehringer UV-test combination adapted to 1 mul PL. The lactate concentrations in the PL of scala tympani and scala vestibuli did not differ significantly. The mean values amounted to 4.5-5.2 mM/l in the case of the opened and of the unopened subarachnoid space (Table 1). The lactate concentrations in the PL of both cochlea scales were significantly higher already ten minutes post-mortem. In the exposure experiments the animals were unilaterally exposed to sound for 1 h in an acoustically isolated system using a wide-band noise at an intensity of 120 dB SPL for one series and 2-kHz pure-tone at intensities of 112 and 122 dB SPL for two other series. We did not detect any changes in the lactate concentrations neither in the PL nor in the blood and in the CSF, following sound exposure (Table 2 and 3). The lactate concentrations of arterial and venous blood and CSF did not differ significantly. The mean values amounted to 1.4-1.8 mM/l (Table 2). However, if blood was not deproteinized or centrifuged immediately after being taken, the lactate concentration increased markedly. A comparison of the present results has shown that the lactate concentration in the PL is about three times as high as in blood and in CSF. This difference in concentration suggests that the PL lactate is of intracochlear origin and that glycolytic processes take place in the inner ear also under normal conditions. Systematic studies of additional metabolic parameters must be conducted before a definitive physiological interpretation of the present analytical results can be given.

Animals↗
PubMed1976

[Otitis media and cochlea. Morphological and biochemical studies in guinea pigs (author's transl)].

The paper deals with: 1. the protein concentration in the perilymph (PL), the serum and the cerebrospinal fluid (CSF), 2. the protein pattern in the PL and 3. histological findings in the middle and inner ear in unilaterally ear-infected guinea pigs. The studies were performed 6 h to 21 days post infectionem (Fig. 1). The pathological changes in the middle ear, which, in most cases, were limited to the infected ear, were initially evaluated under the operating microscope and divided into 4 stages. The analytical and histological results were presented as functions of these stages. As the inflammation intensity increased, the protein concentration in the PL of the infected ears increased to a level exceeding that of the normal value more than ten times (Fig. 2). However, in the serum and in the CSF this concentration remained unchanged. Likewise, no significant protein increase in the PL of the contralateral ears was detectable in most cases. As the inflammation intensity increased, the number of the precipitation lines detectable immunoelectrophoretically increased in the PL of the infected ears (Fig. 3). An increase in the alpha1- and gamma-globulins and a decrease in Albumin was found by electrophoresis on cellulose acetate strips (Tab. 3). The histological findings correlated with initially established inflammatory stages of the middle ear mucous membrane (Tab. 4). As the inflammation intensity increased, the round window, too, was changed pathologically, so that in some cases of purulent otitis media middle ear secretion could enter the cochlea. The protein increase in the PL immediately after the infection is probably due to an increase in the blood vessel permeability in the inner ear.

Animals↗
PubMed1976

Crystallographic structural studies of a human Fc-fragment. I. An electron-density map at 4 A resolution and a partial model.

The crystal structure of a human Fc fragment was analysed at 4 A resolution. A partial interpretation of the electron-density map in terms of domain structure was possible. The molecule has the shape of a mickey mouse. The spherical domain was interpreted visually and by domain Patterson function interpretation as the CH3 dimer. This dimer resembles closely the CH1-CL dimer found in Fab structures. The ellipsoidal "ears" of the molecule represent the CH2 domains. They are widely separated from each other, but closely connected to CH3. Their tertiary structure must be different from CH1, as Patterson domain interpretations were unsuccessful. A chain tracing in CH2 was not yet possible.

Crystallography↗
PubMed1975

[Isolation and characterization of a 19S-alpha1-glycoprotein from human erythrocytes and its identification as placenta protein PP6].

A high molecular weight protein was isolated from the hemolysate of washed human erythrocytes by a procedure involving ion exchange chromatography, ammonium sulfate fractionation and gel filtration. The purified protein was found to have a sedimentation coefficient of 18,68S and a molecular weight of 8 times 10-5 to 1 times 10-6 daltons. In the presence of sodium dodezylsulfate the molecules are dissociated into at least four different subunits having molecular weights ranging from 12,000 to 30,000 daltons. The protein has the electrophoretic mobility of an alpha-1-globulin and an isoelectric point of pH 4.75. The chemical analysis revealed that the protein is chemical and immunochemical properties the 19S-alpha-1-glycoprotein from human erythrocytes was shown to be identical with the protein PP6 isolated from huamn placentae. The content of this protein in packed red blood cells was determined to be around 50 mg per 100 ml.

Chromatography, Gel↗
PubMed1975

[Congenital leucosis with unusual involvement of the brain(author's transl)].

A case of congenital paraleucoblast-leucosis is reported. The diagnosis rested on pronounced infiltrations of the skin and leucemic signs in blood and bone marrow. The child died on the 20th day after developing signs of bleeding and cerebral involvement. At necropsy leucotic infiltration was found in may organs, mainly in pancreas, skin and bone marrow. The most prominent findings and cause of death were diffuse hemorrhagic foci with a high proportion of leucemic cells in the brain and cerebellum.

Acute Disease↗
PubMed1975

[Isolation of beta2-microglobulin from human colostrum (author's transl)].

The beta2-microglobulin from human colostrum was purified by a combination of ordinary protein-chemical techniques: gel filtration, ion-exchange chromatography and zone electrophoresis. The procedure is organized in such a way that the simultaneous isolation of many other milk proteins is possible. The beta2-microglobulin obtained from colostrum cannot be distinguished by physical-chemical or immunological means from the beta2-microblobulin isolated from the urine of patients with kidney-tubule diseases. At the beginning of lactation, human milk contains significantly more than 10 mg/-100 ml beta2-microglobulin, but the concentration drops within two or three days to 15-30% of the original amount.

Beta-Globulins↗