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Biomedical subjects

B Hultberg

Publications and source records attributed to B Hultberg.

At least 19 recordsLinked to original sources
PubMed1979

Isoelectric focusing of acid hydrolases in human fibroblasts and leucocytes.

Lysosomal hydrolases in fibroblasts and leucocytes exhibited the same isoelectric focusing pattern as found in liver. Treatment with neuraminidase had a great effect on the pattern of several glycosidases while treatment with alkaline phosphatase did not significantly change the pattern. These findings are discussed with special reference to the different "uptake" systems that exist for acid hydrolases.

Acetylglucosaminidase↗
PubMed1979

Neonatal non-ketotic hyperglycinemia: a clinical, biochemical and neuropathological study including electronmicroscopic findings.

In a family of four children, three died within 8 days after birth. The fourth child survived after a critical first week with the same symptoms as the siblings. He was at the age of four found to have non-ketotic hyperglycinemia. The histories and neuropathology of the other children were then reexamined. It seems highly probable that all siblings suffered from non-ketotic hyperglycinemia. This report points to the clinical, biochemical and neuropathological diagnostic problems in this disease and also adds new information on the ultrastructural changes, not hitherto visualized.

Amino Acid Metabolism, Inborn Errors↗
PubMed1979

Lysosomal hydrolases in CSF of patients with multiple sclerosis.

The activities of acid phosphatase and N-acetyl-beta-glucosaminidase have been measured in 171 samples of cerebrospinal fluid from 104 patients suffering from multiple sclerosis. The mean level of activity of these enzymes was lower than of controls. Patients who had the first or second bouts had somewhat higher activity of these enzymes compared to controls. The lowest values of these enzymes were found in patients with severe disability. Patients with late onset of the disease had higher levels of the enzymes compared to patients with an earlier debut of the illness, whereas patients with a short history had higher values than patients with a longer duration.

Acetylglucosaminidase↗
PubMed1979

A new N-acetyl-beta-D-hexosaminidase disease with late onset of progressive neurological symptoms.

Clinical data are presented on a 30-year-old male with normal early development (4-5 years) but subsequent progressive impairment of psychomotor functions. He has marked kyphoscoliosis and talipes calcaneo-valgus. The organs appear normal and the patient can walk unaided and feed himself although he does not recognize his parents. He has normal fundi oculi. Biochemical data show an absence of mucopolysacchariduria and very low but detectable levels of N-acetyl-beta-D-hexosaminidase in serum and leucocytes. The clinical symptoms are much milder than would normally be expected from such a profound enzyme deficiency (Sandhoff disease).

Adult↗
PubMed1979

Metabolism of mannose and fucose in cultured fibroblasts from patients with mannosidosis and mucolipidosis.

The incorporation of 14C-D-mannose or 14C-L-fucose into cultured fibroblasts from controls and patients with mannosidosis and mucolipidosis type II was studied. Mannose-containing oligosaccharide chains retarded on Sephadex G-25 were accumulated in cells from both patients. Fucose-containing oligosaccharides retarded on G-25 were also accumulated in cells from the patient with mucolipidosis. Besides there was an increase of macromolecular fucose-containing material in the cells from the patient with mucolipidosis. Conditioned medium of the cells from controls and the different patients exhibited about the same pattern as found in the cells, which might indicate leakage of the cellular material due to cell damage or death.

Carbohydrate Metabolism, Inborn Errors↗
PubMed1979

Fluorometric assay of the arylsulphatases in human urine.

A method is described which differentiates arylsulphatase A and arylsulphatase B in human urine. 4-Methylumbelliferyl sulphate serves as the substrate, and silver ions are used to inhibit arylsulphatase A activity. Using fresh urine it is possible to obtain separate values for arylsulphatase A and B when both are present, thus providing a diagnostic test for metachromatic leucodystrophy.

Cerebroside-Sulfatase↗
PubMed1979

Intestinal lysosomal enzymes in the diagnosis of pancreatic disease.

Acid hydrolases (lysosomal enzymes) were analyzed and compared with trypsin in duodenal juice obtained after a test meal (Lundh test). The possible diagnostic role of acid hydrolases in pancreatic disease was investigated. In all patients with chronic pancreatitis normal values of acid hydrolases but subnormal trypsin activities were found. In pancreatic cancer normal values of acid hydrolases and normal trypsin values were seen in three patients with small tumors, whereas five patients with more advanced cancer of the pancreas had decreased trypsin activity and three of them high activities of acid hydrolases in duodenal juice. In five patients operated on with a gastroenteroanastomosis acid hydrolases were markedly increased. Five patients had no activity of acid hydrolases in the aspirate, probably reflecting technical failure with dislodgement of the catheter from the duodenum to the stomach. In conclusion the assay of acid hydrolases does not seem to increase the diagnostic value of the conventional Lundh test (trypsin).

Acetylglucosaminidase↗
PubMed1978

Isoelectric focusing of acid hydrolases in human liver and serum. Findings in sera from one patient with I-cell disease phenotype.

Isoelectric focusing was performed with six acid hydrolases in serum and liver tissue. Neuraminidase-treated serum and liver tissue were also examined. In general, acid hydrolases in sera seemed to be more sialylated than those in liver tissue. Serum from one patient with I-cell disease with increased activity of some acid hydrolases was found to have a normal isoelectric focusing pattern. These findings are discussed with respect to the uptake mechanism of acid hydrolases in serum.

Female↗
PubMed1978

An atypical form of Sandhoff's disease. Case report and biochemical studies.

A case of Sandhoff's disease (GM2 gangliosidosis type 2) is reported because of an unusual course with later onset of symptoms, more slow progress and longer survival than those previously described. Otherwise the patient presented most of the classical symptoms of the disease with a final state of blindness, deafness and decerebrate rigidity. The residual acidic hexosaminidase isozymes in liver and brain tissue were Hex A and Hex S, while Hex B was barely detectable. The neutral hexosaminidase form called Hex C was also found. Two urinary oligosaccharides containing N-acetylglucosamine and mannose were found to be execreted by the patient.

Acetylglucosaminidase↗
PubMed1978

beta-Glucosidase activities in the Norrbotten type of juvenile Gaucher's disease.

beta-Glucosidase and N-acetyl-beta-glucosaminidase activities were measured with synthetic substrates in peripheral leucocytes, urine and serum from patients with juvenile type of Gaucher's disease. Our findings in urine and serum make it clear that diagnosis by using synthetic substrate is not possible. In peripheral leucocytes reduced level was found for beta-glucosidase activity in patients with Gaucher's disease but also there occurred some overlapping with controls. The possible explanation to these findings are discussed.

Gaucher Disease↗
PubMed1978

beta-D-galactosidase activities in juvenile GM1-gangliosidosis.

beta-Galactosidase activity was investigated in one case of juvenile GM1-gangliosidosis. This patient exhibited normal activity of the neutral form of beta-galactosidase (measured as beta-glucosidase activity) and normal pH curve of residual acid beta-galactosidase activity in leucocytes and fibroblasts. A shift towards more neutral pH optimum was seen in the beta-galactosidase enzyme occurring in serum. The communication also presents a study of the relationship of the different beta-galactosidases in human liver using isolated urine oligosaccharide from this patient as a beta-galactoside substrate. The other natural beta-galactoside substrates used in this investigation were different oligosaccharides, one glycopeptide and ceramide-beta-galactosidase. The beta-galactosidase forms with acidic pH optimum towards synthetic substrate (A forms) exhibit activity towards the natural substrate (except ceramide-beta-galactoside). The "neutral" beta-galactosidase with broad substrate specificity (B form) which includes beta-glucosides had no activity towards the natural substrates used. It could also be shown that the activity towards ceramide-beta-galactoside was a third type of beta-galactosidase different from A and B forms.

Adolescent↗
PubMed1978

Diagnostic value of determinations of lysosomal hydrolases in CSF of patients with neurological diseases.

The activities of four lysosomal acid hydrolases, beta-galactosidase, alpha-mannosidase at pH 4.5 and 5.5, N-acetyl-beta-glucosaminidase, and acid phosphatase, have been measured in serum and cerebrospinal fluid from 179 patients with different neurological diseases and from 20 healthy controls. In patients with tumours, decreased activity of beta-galactosidase was found in both serum and cerebrospinal fluid, and in patients with multiple sclerosis and collagen diseases, decreased activities of beta-galactosidase and N-acetyl-beta-glucosaminidase were found in cerebrospinal fluid. The variations of enzyme activities were great between the individual patients even with these groups and analysis of lysosomal enzymes seems to have a very poor clinical value.

Acetylglucosaminidase↗
PubMed1977

A comparison of the alpha-L-fucosidase activities of human liver and serum.

Human liver alpha-L-fucosidase (alpha-L-fucoside fucohydrolase, EC 3.2.1.51) has been separated into four components by chromatography on Sephadex G-150 or DEAE-cellulose. These components differ in their relative stability to heat and acid treatment, and their response to neuraminidase. The serum enzyme was devoid of high molecular weight activity and probably contained more sialic acid residues than the corresponding enzyme from liver. All the liver components tested were able to liberate fucose from 2'-fucosyllactose but not fucose from other oligosaccharides.

Chromatography, DEAE-Cellulose↗
PubMed1977

Comparative activity of sulphatases in human liver on two synthetic substrates.

Ion-exchange chromatography and gel chromatography manifested the presence of three different forms of sulphatase activity in human liver using 4-methylumbelliferyl sulphate as substrate. Studies with the substrate 4-nitrocatechol sulphate and inhibition experiments with AgNO3 were also performed on these three different forms of sulphatases. This makes it possible to identify the three forms as arylsulphatase A, B, and C. The conclusion is drawn that the 4-methylumbelliferyl sulphate substrate is inadequate to measure the lysosomal arylsulphatases A and B, but it could be used to measure the microsomal arylsulphatase C.

Catechols↗
PubMed1977

Lysosomal enzymes in medium from cultured skin fibroblasts from normal individuals and patients with lysosomal diseases.

The release of acid hydrolases from cultured skin fibroblasts into the cell culture medium was studied in several lysosomal storage disorders (GM1-gangliosidosis, Fabry's disease, Hurler's disease, mannosidosis, and mucolipidosis). The levels of different activities were proportional to time (up to 44 h after medium change) and cell density with the exception of beta-glucosidase, which was not released. Culture medium from the fibroblasts of mucolipidosis patients exhibited higher activity of acid hydrolases than medium from cells of patients with GM1-gangliosidosis, Fabry's disease, Hurler's disease, and mannosidosis. These cells, however, exhibited somewhat higher levels of enzyme activity in their culture medium than control fibroblasts. The total production of acid hydrolases was yet rather similar in fibroblasts from controls and patients. Differential centrifugation showed that the highest specific activity of acid hydrolases was seen, as expected, in the lysosomal fraction, except in fibroblasts from patients with mucolipidosis, where the supernatant exhibited most activity. beta-Glucosidase, however, showed a normal differential centrifugation pattern also in fibroblasts from these patients.

Carbohydrate Metabolism, Inborn Errors↗
PubMed1976

Neutral alpha-mannosidase activity in human serum.

Two types of alpha-mannosidase (alpha-D-mannoside mannohydrolase, EC 3.2.1.24) with neutral pH optima exist in serum. The activity with an optimum between pH 6.0 and 6.4 is similar to alpha-mannosidase C, described earlier in tissues. The second activity, with a pH optimum between pH 5.2 and 5.8 is the dominant form in serum. These two forms can be differentiated from each other by gel-filtration, chromatography on DEAE-cellulose or chromatography on Concanavalin-A Sepharose. Using the chromatographic techniques, the serum type neutral activity co-elutes with the acidic forms of the enzyme. However, these two forms can be easily distinguished by effect of pH, heating or inhibition by the substrate methyl-alpha-D-mannopyranoside. The presence of the serum type alpha-mannosidase activity is discussed with respect to mannosidosis, a lysosomal storage disease.

Disaccharidases↗