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amyloidosis/carbohydrate
Link salvestatakse lõikelauale
Leht 1 alates 276 tulemused
Topo-optical visualization reactions of carbohydrate-containing amyloid deposits in the respiratory tract.
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Staining with Congo red according to is the most commonly used method for the demonstration of amyloid, but structures other than amyloid can give false-positive results. To overcome this problem, introduced an aqueous Congo red staining with gum arabic as the mounting medium, which we have used in
Abnormal serum carbohydrate antigen 19-9 levels in a patient with splenic retiform haemangioendothelioma concomitant with hepatic amyloidosis: A case report.
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Structural studies of a carbohydrate-containing immunoglobulin-lambda-light-chain amyloid-fibril protein (AL) of variable subgroup III.
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The amino acid sequence of the variable region of a carbohydrate-containing amyloid-fibril protein MOL of immunoglobulin-light-chain type (AL) was elucidated. The sequence determination involved cleaving the protein with CNBr, BNPS-skatole, thermolysin and trypsin. The sequenced protein consisted of
The carbohydrate composition of human serum amyloid P component.
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The carbohydrate moiety of human serum amyloid P component was analyzed and found to consist of equal amounts of galactose and mannose (total 4.0%), of glucosamine and galactosamine in a ratio of 7:1 (total 2.7%) and sialic acid (3.9%). It should be noted that this is the first report on the
Taurine-Carbohydrate Derivative Stimulates Fibrillogenesis of Amyloid-β and Reduce Alzheimer-Like Behaviors.
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Amyloid-β (Aβ) aggregates are a hallmark of Alzheimer's disease (AD). Through the misfolding process of Aβ in the brain, oligomeric forms of Aβ accumulate and significantly damage the brain cells inducing neuronal loss and cognitive dysfunctions that lead to AD. We hypothesized that decrease in Aβ
Carbohydrate histochemistry of amyloid plaques in Gerstmann-Sträussler syndrome.
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Prion proteins and sulfated glycosaminoglycans are known to be components of PAS-positive amyloid plaques in Creutzfeldt-Jakob disease, Gerstmann-Sträussler syndrome, and kuru. Using a panel of fluorescein labeled lectins the terminal carbohydrate residues of amyloid plaques in two patients with
Microheterogeneity of serum glycoproteins and their liver precursors in patients with carbohydrate-deficient glycoprotein syndrome type I: apparent deficiencies in clusterin and serum amyloid P.
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Serum and liver protein patterns were studied, respectively, in 5 patients (serum) and 1 patient (liver) with carbohydrate-deficient glycoprotein syndrome (CDGS) type I by high-resolution two-dimensional electrophoresis (2-DE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Lack of islet amyloid polypeptide/amylin-immunoreactivity in urine collected from healthy volunteers after ingestion of a carbohydrate-rich meal.
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Islet amyloid polypeptide (IAPP), or amylin, is synthesized by beta cells in the islets of Langerhans of the pancreas. Plasma IAPP levels are highly elevated in patients with advanced renal failure. To investigate the involvement of the kidney in the clearance of IAPP, the response of plasma and
The amino acid sequence of a carbohydrate-containing immunoglobulin-light-chain-type amyloid-fibril protein.
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The amino acid sequence of an amyloid-fibril protein Es492 of immunoglobulin-lambda-light-chain origin (AL) was elucidated. The amyloid fibrils were obtained from the spleen of a patient who died from systemic amyloidosis. The amino acid sequence was elucidated from structural studies of peptides
The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS (immunoglobulin light chain, type lambda).
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The amino-acid sequence of the variable region of a carbohydrate-containing amyloid fibril protein EPS of immunoglobulin lambda light chain origin has been elucidated. The protein was isolated from the liver of a patient (EPS) with an immunocyte dyscrasia of the IgM type. The molecular mass of this
Use of capillary zone electrophoresis to evaluate the binding of anionic carbohydrates to synthetic peptides derived from human serum amyloid P component.
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Capillary zone electrophoresis was used to study interactions between anionic carbohydrates and synthetic peptides derived from the heparin-binding region of human serum amyloid P component. The method involves quantitation of unbound peptides after a charge-dependent electrophoretic separation of
The structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose.
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Two monoclinic (P2(1)) crystal forms of human serum amyloid P component (SAP) in complex with the 4,6-pyruvate acetal of beta-D-galactose (MObetaDG) were prepared. Structure analysis by molecular replacement and refinement at 2.2A resolution revealed that crystal form 1 (a=95.76A, b=70.53A,
Serum amyloid P-component/C-reactive proteins in fugu (Takifugu rubripes) egg with binding ability to disease-causing bacteria by carbohydrate-recognition
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Two galactose-binding proteins were purified from the eggs of Takifugu rubripes by affinity chromatography. These proteins were detected at 26 and 23 kDa under reducing and at 40 and 45 kDa under non-reducing conditions at SDS-PAGE. The peptide sequences from both proteins matched to short-type
[Comparative studies on the histochemical behavior of amyloid, fibrinoid and hyalin deposits in blood vessel walls in mammals and birds. II. Carbohydrates].
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Serum proteins and protein-bound carbohydrates in tuberculosis and amyloidosis.
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