Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Biosynthesis, processing, and extracellular release of α-l-fucosidase in lymphoid cell lines of different genetic origins (1988)
    Springer
    Biochemical genetics 26 (1988), S. 401-420 
    Details
    ISSN: 1573-4927
    Keywords: α-l-fucosidase ; lymphoid cells ; fucosidosis ; serum polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In humans, the quantity of α-l-fucosidase in serum is determined by heredity. The mechanism controlling levels of the enzyme in serum is unknown. Lymphoid cell lines derived from individuals with either low, intermediate, or high α-l-fucosidase in serum were established. Steady-state levels of intracellular and extracellular α-l-fucosidase as well as rates of synthesis and secretion of enzyme overlapped among the cell lines. Thus,vivo} serum phenotypes were not expressed in this system. No appreciable differences in the qualitative processing of newly made α-l-fucosidase were observed among these lymphoid cell lines. Cells pulse-labeled with35S-methionine from 0.25 to 2 hr had an intracellular form of enzyme with aM r=58,000. Cells pulsed for 1.5 hr and chased for 21 hr with unlabeled methionine had an intracellular form ofM r=60,000 and an extracellular form ofM r=62,000. All three enzyme forms were glycoproteins with a common polypeptide chain ofM r=52,000 but with different carbohydrate moieties. No evidence for a high molecular mass precursor form of α-l-fucosidase was found. Fucosidosis is a rare, inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The mutations for fucosidosis and the serum polymorphism map separately. Lymphoid cells from two siblings with fucosidosis had 8-fold to 341-fold less intracellular α-l-fucosidase protein with 11-fold to 56-fold lower specific activities than control cells. Residual mutant enzyme was a glycoprotein with a polypeptide chain virtually the same size (M r=52,000) as control enzyme. However, residual mutant enzyme was hypoglycosylated and hypersecreted as compared to control enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554076
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Biosynthesis, processing, and extracellular release of α-l-fucosidase in lymphoid cell lines of different genetic origins (1988)
    Springer
    Biochemical genetics 26 (1988), S. 401-420 
    Details
    ISSN: 1573-4927
    Keywords: α-l-fucosidase ; lymphoid cells ; fucosidosis ; serum polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In humans, the quantity of α-l-fucosidase in serum is determined by heredity. The mechanism controlling levels of the enzyme in serum is unknown. Lymphoid cell lines derived from individuals with either low, intermediate, or high α-l-fucosidase in serum were established. Steady-state levels of intracellular and extracellular α-l-fucosidase as well as rates of synthesis and secretion of enzyme overlapped among the cell lines. Thus,vivo} serum phenotypes were not expressed in this system. No appreciable differences in the qualitative processing of newly made α-l-fucosidase were observed among these lymphoid cell lines. Cells pulse-labeled with35S-methionine from 0.25 to 2 hr had an intracellular form of enzyme with aM r=58,000. Cells pulsed for 1.5 hr and chased for 21 hr with unlabeled methionine had an intracellular form ofM r=60,000 and an extracellular form ofM r=62,000. All three enzyme forms were glycoproteins with a common polypeptide chain ofM r=52,000 but with different carbohydrate moieties. No evidence for a high molecular mass precursor form of α-l-fucosidase was found. Fucosidosis is a rare, inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The mutations for fucosidosis and the serum polymorphism map separately. Lymphoid cells from two siblings with fucosidosis had 8-fold to 341-fold less intracellular α-l-fucosidase protein with 11-fold to 56-fold lower specific activities than control cells. Residual mutant enzyme was a glycoprotein with a polypeptide chain virtually the same size (M r=52,000) as control enzyme. However, residual mutant enzyme was hypoglycosylated and hypersecreted as compared to control enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02401794
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Specific activity of α-l-fucosidase in sera with phenotypes of either low, intermediate, or high total enzyme activity and in a fucosidosis serum (1986)
    Springer
    Biochemical genetics 24 (1986), S. 115-130 
    Details
    ISSN: 1573-4927
    Keywords: specific activity ; α-l-fucosidase ; serum polymorphism ; fucosidosis ; enzyme-linked immunoabsorbent assay (ELISA)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The quantity of α-l-fucosidase activity in human serum is determined by heredity. An individual may inherit either low, intermediate, or high serum enzyme activity. An enzyme-linked immunoabsorbent assay has been developed that can detect 0.3 ng of α-l-fucosidase protein. Enzyme protein in serum of 102 individuals ranged from 20 to 835 ng/ml. The group included individuals with low, intermediate, and high enzyme activity. The specific activity of α-l-fucosidase within this group was statistically the same (mean±SD=11,002±1051 U/mg). Thus, individuals with low and intermediate enzyme activity in serum had lower amounts of enzyme protein with the same specific activity as in individuals with high enzyme activity. Fucosidosis is a rare inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The concentrations of enzyme protein in sera of a fucosidosis patient and parents were 76, 565, and 604 ng/ml, respectively, and the specific activities of enzyme were 1316, 8938, and 8858 U/mg, respectively. Thus, the fucosidosis serum probably contained a structurally altered enzyme with reduced catalytic activity. The somewhat low specific activities in the parents suggested that their sera contained both structurally altered and normal protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00502983
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Brain monoamines after portacaval anastomosis (1986)
    Springer
    Metabolic brain disease 1 (1986), S. 45-52 
    Details
    ISSN: 1573-7365
    Keywords: hepatic encephalopathy ; high-performance liquid chromatography ; liver disease ; monoamine neurotransmitters ; portacaval shunting ; rats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Norepinephrine, dopamine, and serotonin, as well as the serotonin metabolite, 5-hydroxy-indoleacetic acid, were measured in whole-brain extracts from rats with a portacaval shunt or sham operation. Norepinephrine, serotonin, and 5-hydroxyindoleacetic acid were significantly higher after shunting. There was no difference in dopamine. The results support the idea that brain indole metabolism is increased during chronic hepatic encephalopathy. However, they provide evidence against suggestions that hepatic encephalopathy in general is accompanied by a shortage in the whole-brain content of the catecholamines norepinephrine and dopamine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00998476
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Regional blood-brain barrier transport of glucose after portacaval anastomosis (1986)
    Springer
    Metabolic brain disease 1 (1986), S. 119-128 
    Details
    ISSN: 1573-7365
    Keywords: glucose transport ; blood-brain barrier ; regional glucose utilization ; portacaval anastomosis ; hepatic encephalopathy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The regional influx of glucose across the blood-brain barrier was measured in rats 5 to 6 weeks after a portacaval anastomosis or sham operation. D-[14C]Glucose was infused intravenously for 15sec while arterial blood was sampled continuously for measurement of plasma radioactivity and glucose concentration. Brain tissue radioactivity was measured by quantitative autoradiography. Glucose influx and plasma clearance (permeability times surface area;PS) were calculated from the net disintegrations per minute per gram in brain, the plasma radioactivity integral, and the plasma glucose concentration. In shunted rats influx was decreased by about 22% (in the brain as a whole) compared to that in controls. This decrease was almost entirely due to the decrease in plasma glucose concentrations (27%). ThePS, normalized to take plasma concentrations into account, showed a slight decrease in most of the brain except the telencephalon. For the brain as a whole this decrease amounted to 11%. The regionalPS and glucose utilization are known to be coupled and the relationship between these was the same in sham-operated and shunted rats. The decrease inPS observed in shunted rats was commensurate with their lower rates of glucose use; thus, the transport process of glucose from plasma to brain appeared to be unaffected by portacaval shunting.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00999382
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...