Results 1 to 10 of about 392,626 (135)

The Enzymatic Degradation of Heparin and Heparitin Sulfate

open access: hybridJournal of Biological Chemistry, 1965
Crude enzyme obtained from heparin-induced flavobacteria has been fractionated into a heparitinase acting on heparitin sulfates and related compounds and a heparinase acting mainly on heparin. Purification achieved for each was from 50 to 100 times that of earlier preparations containing a mixture of the two enzymes.
Alfred Linker, Peter Hovingh
semanticscholar   +8 more sources

Heparitin Sulfate Mucopolysaccharidosis (Sanfilippo Disease): A Case Study with Ultrastructural, Biochemical, and Radiological Findings [PDF]

open access: bronzePediatric Research, 1971
Extract: A case study of a 14-year-old female child who developed normally for 18 months but subsequently deteriorated rapidly in mental status and social behavior is reported. Histochemical studies of tissues removed at biopsy from liver, skin, and bone marrow showed changes similar to those found in the Hurler syndrome. Ultrastructural changes of the
M. Daria Haust   +9 more
semanticscholar   +3 more sources

Structural Studies on Heparitin Sulfate of Normal and Hurler Tissues

open access: hybridJournal of Biological Chemistry, 1967
Abstract Heparitin sulfate isolated from human aorta is a polysaccharide of molecular weight 24,000 to 29,000, which is bound to protein by way of serine. The presence of serine, xylose, and galactose in a molar ratio of 1:1:2 suggests that the linkage region of this mucopolysaccharide is similar to that in chondroitin 4-sulfate and in heparin ...
Albert Dorfman   +2 more
semanticscholar   +5 more sources

Effect of Heparitin Sulfate Fractions on Coagulation and Hemostasis

open access: closedExperimental Biology and Medicine, 1974
SummaryThe antihemostatic and anticoagulant activities of heparin and heparitin sulfate fractions were compared. Heparitin sulfate D has the same antihemostatic activity as heparin but negligible anticoagulant activity, demonstrating differences in the molecular mechanisms of these two biological processes.
Carl P. Dietrich, Helena B. Nader
semanticscholar   +5 more sources

The identification of proteoglycans and glycosaminoglycans in archaeological human bones and teeth [PDF]

open access: yes, 2015
Bone tissue is mineralized dense connective tissue consisting mainly of a mineral component (hydroxyapatite) and an organic matrix comprised of collagens, non-collagenous proteins and proteoglycans (PGs).
A Hildebrand   +70 more
core   +2 more sources

Identification of acid mucopolysaccharides by paper chromatography [PDF]

open access: yes, 1964
A multiple solvent paper chromatography system is described which tentatively identifies most of the known mammalian acid mucopolysaccharides, when these are examined singly.
Dorstewitz, Emily L., William Castor, C.
core   +1 more source

Shear Stress Induces the Release of an Endothelial Elastase: Role in Integrin alpha(v)beta(3)-Mediated FGF-2 Release [PDF]

open access: yes, 2011
Background/Aims: Laminar shear stress is an important stimulus in the endothelium-dependent control of vascular tone and of vascular remodeling processes.
Gloe, Torsten   +4 more
core   +1 more source

Síndrome de Sanfilippo [PDF]

open access: yes, 2022
Sanfilippo syndrome or mucopolysaccharidosis III is an automosal recessive genetic disease, where there is an alteration in the enzymes responsible for the metabolism of long sugar chains, called glucominoglycans (mucopolysaccharides).
Rappaccioli Salinas, Renata
core   +2 more sources

Cathepsin B-associated Activation of Amyloidogenic Pathway in Murine Mucopolysaccharidosis Type I Brain Cortex [PDF]

open access: yes, 2020
Mucopolysaccharidosis type I (MPS I) is caused by genetic deficiency of alpha-l-iduronidase and impairment of lysosomal catabolism of heparan sulfate and dermatan sulfate.
Baldo, G   +9 more
core   +2 more sources

Sanfilippo syndrome: molecular basis, disease models and therapeutic approaches [PDF]

open access: yes, 2022
Sanfilippo syndrome or mucopolysaccharidosis III is a lysosomal storage disorder caused by mutations in genes responsible for the degradation of heparan sulfate, a glycosaminoglycan located in the extracellular membrane.
Benetó, Noelia   +3 more
core   +1 more source

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