ChemInform Abstract: BIMETALLIC COPPER(I) AND -(II) MACROCYCLIC COMPLEXES AS MIMICS FOR TYPE 3 COPPER PAIRS IN COPPER ENZYMES

1979 ◽  
Vol 10 (40) ◽  
Author(s):  
Y. AGNUS ◽  
R. LOUIS ◽  
R. WEISS
Keyword(s):  
Macrocyclic Complexes ◽  
Copper Enzymes ◽  
Type 3

Thiomethyl Substituted Dicopper Complexes: Attempts to Reproduce the Asymmetry of the Active Site from Type 3 Copper Enzymes

2013 ◽  
Vol 639 (8-9) ◽  
pp. 1477-1482 ◽  
Author(s):  
Wassim Rammal ◽  
Katalin Selmeczi ◽  
Christian Philouze ◽  
Eric Saint-Aman ◽  
Jean-Louis Pierre ◽  
...  
Keyword(s):  
Active Site ◽  
Copper Enzymes ◽  
The Asymmetry ◽  
Type 3 ◽  
Dicopper Complexes

Scanning Electron Microscopy of the Red Pulp of the Spleen

1971 ◽  
Vol 29 ◽  
pp. 496-497
Author(s):  
Masayuki Miyoshi
Keyword(s):  
Electron Microscope ◽  
Ringer Solution ◽  
Conclusive Evidence ◽  
Sinus Wall ◽  
Transmission Electron ◽  
Type 3 ◽  
Cytoplasmic Processes ◽  
Splenic Red Pulp ◽  
Scanning Electron ◽  
Red Pulp

In spite of various attempts, conclusive evidence to explain blood passage in the splenic red pulp does not seem to have been presented. Scanning electron microscope (SEM) observations on the rabbit spleen, originally performed by us, revealed that the sinus was lined by a perforated lattice composed of longitudinally extended rod cells and transverse cytoplasmic processes, and that perforations in the lattice were continuous to the spaces among the stellate reticulum cells of the cord. In the present study the observation was extended to the dog and rat spleens, in which the cord is more developed than in the rabbit in order to clarify the possible differences in the fine structure of the sinus wall. An attempt was also made to examine the development and distribution of macrophage in the blood passage of the red pulp.Spleens were washed and fixed by perfusion with Ringer solution and then with buffered glutaraldehyde. Small tissue cubes were dehydrated with acetone, dried in air and heated with gold. Observations were made by a JEOL SEM Type-3. One air dried tissue cube was cut into small pieces and post fixed with buffered OsO4 for examination under the transmission electron microscope (TEM).

Familial hyperlipoproteinemia type 3

1969 ◽  
Vol 100 (4) ◽  
pp. 401-406 ◽  
Author(s):  
R. Fleischmajer
Keyword(s):  
Type 3

Ten years’ experience of enzyme infusion therapy of Norrbottnian (type 3) Gaucher disease

2006 ◽  
Vol 95 (3) ◽  
pp. 312-317 ◽  
Author(s):  
Anders Erikson ◽  
Håkan Forsberg ◽  
Magnus Nilsson ◽  
Marianne Åström ◽  
Jan-Eric Månsson
Keyword(s):  
Gaucher Disease ◽  
Infusion Therapy ◽  
Type 3 ◽  
Enzyme Infusion

A Novel Mutation Glyl672→Arg in Type 2A and a Homozygous Mutation in Type 2B von Willebrand Disease

1996 ◽  
Vol 76 (02) ◽  
pp. 253-257 ◽  
Author(s):  
Takeshi Hagiwara ◽  
Hiroshi Inaba ◽  
Shinichi Yoshida ◽  
Keiko Nagaizumi ◽  
Morio Arai ◽  
...  
Keyword(s):  
Missense Mutation ◽  
Novel Mutation ◽  
Point Mutations ◽  
Japanese Patients ◽  
Von Willebrand Disease ◽  
Homozygous Mutation ◽  
Missense Mutations ◽  
Reaction Products ◽  
Type 3 ◽  
Von Willebrand

SummaryGenetic materials from 16 unrelated Japanese patients with von Willebrand disease (vWD) were analyzed for mutations. Exon 28 of the von Willebrand factor (vWF) gene, where point mutations have been found most frequent, was screened by various restriction-enzyme analyses. Six patients were observed to have abnormal restriction patterns. By sequence analyses of the polymerase chain-reaction products, we identified a homozygous R1308C missense mutation in a patient with type 2B vWD; R1597W, R1597Q, G1609R and G1672R missense mutations in five patients with type 2A; and a G1659ter nonsense mutation in a patient with type 3 vWD. The G1672R was a novel missense mutation of the carboxyl-terminal end of the A2 domain. In addition, we detected an A/C polymorphism at nucleotide 4915 with HaeIII. There was no particular linkage disequilibrium of the A/C polymorphism, either with the G/A polymorphism at nucleotide 4391 detected with Hphl or with the C/T at 4891 detected with BstEll.

Evaluation of the Abnormal Platelet Function in von Willebrand Disease by the Blood Filtration Test

1996 ◽  
Vol 76 (03) ◽  
pp. 460-468 ◽  
Author(s):  
Francesco I Pareti ◽  
Marco Cattaneo ◽  
Luca Carpinelli ◽  
Maddalena L Zighetti ◽  
Caterina Bressi ◽  
...  
Keyword(s):  
Platelet Function ◽  
Relevant Information ◽  
Von Willebrand Disease ◽  
Type I ◽  
Cumulative Number ◽  
Primary Hemostasis ◽  
Normal Platelet ◽  
Filter Test ◽  
Type 3 ◽  
Von Willebrand

SummaryWe have evaluated platelet function in different subtypes of von Willebrand disease (vWD) by pushing blood through the capillarysized channels of a glass filter. Patients, including those with type IIB vWD, showed lower than normal platelet retention and increased cumulative number of blood drops passing through the filter as a function of time. In contrast, shear-induced platelet aggregation, measured in the cone-and-plate viscometer, was paradoxically increased in type IIB patients. Treatment with l-desamino-8-D-arginine vasopressin (DDAVP) tended to normalize the filter test in patients with type I-platelet normal and type I-platelet low vWD, but infusion of a factor VUI/von Willebrand factor (vWF) concentrate lacking the largest vWF multimers was without effect in type 3 patients. Experiments with specific monoclonal antibodies demonstrated that the A1 and A3 domains of vWF, as well as the glycoproteins Ibα and Ilb-IIIa on platelets, are required for platelet retention in the filter. Thus, the test may reflect vWF function with regard to both platelet adhesion and aggregation under high shear stress, and provide relevant information on mechanisms involved in primary hemostasis.

Mitochondrial impairment in patients with spinocerebellar ataxia type 3

2004 ◽  
Vol 31 (S 1) ◽  
Author(s):  
L Schöls ◽  
J Andrich ◽  
H Przuntek ◽  
K Müller ◽  
J Zange
Keyword(s):  
Spinocerebellar Ataxia ◽  
Spinocerebellar Ataxia Type ◽  
Spinocerebellar Ataxia Type 3 ◽  
Mitochondrial Impairment ◽  
Type 3
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