PubMed Health⌕ Search

Biomedical subjects

G Lundblad

Publications and source records attributed to G Lundblad.

At least 19 recordsLinked to original sources
PubMed1991

[Lysozyme--an enzyme of both historical and current interest as a therapeutical agent].

Lysozyme, a bacteriolytic protein discovered by Fleming in 1922 and found to be phylogenetically ancient and almost ubiquitous among living organisms, is probably the most studied enzyme in biology and medicine. Evidence of its involvement in resistance to bacterial infection is compelling but remains indirect. Muramyl peptides (fragments of bacterial cell wall peptidoglycan) exert many effects on the immune system and the CNS, and appear to contribute to non-specific resistance to infection, fever, fatigue, and the pathogenesis of bacterial infection. Synthetic muramyl peptide analogues are currently used as adjuvants in vaccine trials in humans. Several pathological conditions are associated with changes in lysozyme concentrations, and egg-white lysozyme treatment has been tried on a small scale. With the cloning of the human lysozyme gene in yeast cells the enzyme can now be produced on a large scale, which will enable its therapeutic applications to be evaluated.

Bacterial Infections↗
PubMed1988

Patterns of glycosidases in the histiocytic cell line U-937. Effects of agents inducing cell differentiation.

1. The cell bound glycosidases in sublines and clones of the histiocytic cell line U-937 have previously been shown to display characteristic patterns. 2. In this paper the effects of differentiation inducing agents upon glycosidase patterns of one subline, U-937 GTB, are presented. 3. Teleocidin, 12-O-tetradecanoyl-phorbol-13-acetate (TPA), dimethyl-sulfoxide (DMSO), dihydroxyvitamin D3 and supernatants from mixed lymphocyte culture (MCL) all induce cellular differentiation of U-937 GTB. 4. Significant changes of the levels of cell bound glycosidases were seen after addition of inducing agents. 5. Alterations have been monitored as relative effects upon the absolute glycosidase activities and as effects upon selected ratios of different glycosidases. 6. The separate inducing agents show distinct enzyme patterns.

Acid Phosphatase↗
PubMed1988

Glycosidase and phosphatase activities in U-937 and some clones and sublines.

1. The activities of nine glycosidases, lysozyme and acid and alkaline phosphatases were compared in the histiocytic lymphoma cell line U-937 and a set of clones and sublines derived from this line. 2. The patterns of the different enzyme activities and selected enzyme ratios have been used as a method to distinguish between different clones and sublines. 3. Sublines with high lysozyme levels were rich in most cell-bound glycosidases. 4. During long-term growth distinct enzyme patterns of individual lines were preserved. 5. The enzyme pattern during a cell culture growth cycle was basically stable.

Acid Phosphatase↗
PubMed1985

Significance of glycosidases and phosphatases in Cercopithecus and Macaca cells.

When selected ratios of different glycosidases and phosphatases from primary monkey kidney cells or from monkey kidney cell lines are presented graphically, characteristic patterns do evolve. Three different subtypes of Vero cells show similar glycosidase patterns. The Vero subtypes tested show glycosidase patterns that are closely similar to those of primary cells of Cercopithecus aethiops. Glycosidase patterns of BS-C-1 and CV-1 cells are less similar to those of primary Cercopithecus cells than are those of Vero cells. Primary kidney cells from Macaca cynomolgus show significantly different glycosidase patterns compared with those of different Cercopithecus cells. The distinct glycosidase patterns can be used to classify the tested cell lines in relation to each other.

Animals↗
PubMed1985

Significance of glycosidase patterns in lymphoid cells.

Characteristic patterns of cell bound lysosomal glycosidases were found in different lymphoblastoid cell lines derived from Epstein-Barr virus-transformed lymphocytes. The enzyme pattern resembled that found in normal lymphocytes from healthy individuals except for a marked increase in alpha-L-fucosidase. beta-D-Glucuronidase on the contrary markedly decreased in the lymphoblastoid cells. Burkitt's lymphoma cells on the other hand showed glycosidase patterns that were quite distinct from those in lymphoblastoid cells. Each lymphoma cell line showed a characteristic pattern. This is one indication of a heterogeneous origin of these tumors. Glycosidase patterns may be used to roughly distinguish different lymphoid cell lines.

Cell Transformation, Viral↗
PubMed1979

Bovine serum chitinase.

1. A glycol-chitin-splitting enzyme without lysozyme (muramidase) activity has been found in calf serum. The enzyme also degrades colloidal chitin and is thus a true chitinase, 1,4-beta-poly-N-acetylglucosaminidase, without exo-beta-N-acetylglucosaminidase effect. 2. The enzyme is purified 1000-fold by ion-exchange chromatography and gel filtration. Its optimal activity is between pH 1.5-2.0 with glycol chitin and between pH 3-6 in a rather broad optimum with colloidal chitin as substrate. The optimal stability of the enzyme is in the pH interval 3.0-6.5 when tested by incubation with glycol chitin at 50 degrees C for 60 min. The optimal temperature for the degradation of glycol chitin is 40 degrees C when assayed at pH 1.5 and 51 degrees C when assayed at pH 3.5. 3. The enzyme is activated by moderate heating at pH 6.5. The highest relative activity, 135% is reached after 45 min incubation at 30 degrees C, pH 5 or after 30 min at 40, pH 2.4. By incubation with small amounts of trypsin at pH 6.5 at 3m degrees C the enzyme was temporarily activated. 4. The isoelectric point, pH 5.3, and the molecular weight, 47,000 +/- 3,000 were determined by respectively isoelectric focusing and gel filtration. 5. The Michaelis-Menten constant, Km = 0.76 +/- 0.05 (S.E.) mg/ml, was measured with glycol chitin as substrate.

Animals↗
PubMed1976

Chitinase and beta-N-acetylglycosaminidase in the digestive juice of Helix pomatia.

A beta-N-acetylglucosaminidase from Helix pomatia digestive juice was separated and partly purified by gel chromatography. The optimal pH for the degradation of p-nitrophenyl-N-acetyl-beta-D-glucosaminide was 3.4. The molecular weight was around 160 000 and the pI = 4.95. In the same gel chromatography run two chitinase active peaks were also obtained. These chitinase active peaks were also obtained. These chitinases, with molecular weights around 26 000 and 13 000, had somewhat different pH activity curves with optima at 4.2 and 4.3. By isoelectric focusing the first peak with molecular weight around 26 000 was divided in two chitinase active regions with pI at 5.7 and 3.5. The second peak with molecular weight around 13 000 had a pI at 7.3.

Acetylglucosaminidase↗