Total Iodide Organification Defect: Clinical and Molecular Characterization of an Italian Family

Thyroid ◽  
2005 ◽  
Vol 15 (9) ◽  
pp. 1085-1088 ◽  
Author(s):  
Laura Fugazzola ◽  
Deborah Mannavola ◽  
Maria Cristina Vigone ◽  
Valentina Cirello ◽  
Giovanna Weber ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Italian Family ◽  
Iodide Organification Defect ◽  
Organification Defect

1446: Molecular Characterization of Cyclooxygenase-2 in a Stimulated Prostate Stroma Cells

2006 ◽  
Vol 175 (4S) ◽  
pp. 467-467
Author(s):  
Victor K. Lin ◽  
Shih-Ya Wang ◽  
Claus G. Roehrbom
Keyword(s):  
Molecular Characterization ◽  
Cyclooxygenase 2 ◽  
Prostate Stroma

Molecular characterization of lincRNAs in Down syndrome associated leukemia

2012 ◽  
Vol 224 (03) ◽  
Author(s):  
A Streltsov ◽  
S Emmrich ◽  
F Engeland ◽  
JH Klusmann
Keyword(s):  
Down Syndrome ◽  
Molecular Characterization

Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding

1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci
Keyword(s):  
Venous Thromboembolism ◽  
Active Site ◽  
Inhibitory Activity ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Molecular Defect ◽  
Affinity Adsorption ◽  
Italian Family ◽  
Crossed Immunoelectrophoresis

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.

Molecular Characterization of Radiation-induced Glioblastoma

2018 ◽  
Author(s):  
MY Deng ◽  
D Sturm ◽  
E Pfaff ◽  
GP Balasubrama ◽  
J Schittenhelm ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Radiation Induced

Clinical and molecular characterization of patients with multiple sulfatase deficiency

2006 ◽  
Vol 37 (06) ◽  
Author(s):  
L Schlotawa ◽  
T Dierks ◽  
K von Figura ◽  
J Gärtner
Keyword(s):  
Molecular Characterization ◽  
Multiple Sulfatase Deficiency

Morphological, histological and molecular characterization of Myxidium cf. rhodei infecting the kidney of Rutilus rutilus

2020 ◽  
Vol 141 ◽  
pp. 39-46
Author(s):  
MD Dorjievna Batueva ◽  
X Pan ◽  
J Zhang ◽  
X Liu ◽  
W Wei ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Molecular Characterization ◽  
Rutilus Rutilus ◽  
Longitudinal Axis ◽  
Suture Line ◽  
Present Species ◽  
Supplementary Data

In the present study, we provide supplementary data for Myxidium cf. rhodei Léger, 1905 based on morphological, histological and molecular characterization. M. cf. rhodei was observed in the kidneys of 918 out of 942 (97%) roach Rutilus rutilus (Linnaeus, 1758). Myxospores of M. cf. rhodei were fusiform with pointed ends, measuring 12.7 ± 0.1 SD (11.8-13.4) µm in length and 4.6 ± 0.1 (3.8-5.4) µm in width. Two similar pear-shaped polar capsules were positioned at either ends of the longitudinal axis of the myxospore: each of these capsules measured 4.0 ± 0.1 (3.1-4.7) µm in length and 2.8 ± 0.1 (2.0-4.0) µm in width. Polar filaments were coiled into 4 to 5 turns. Approximately 18-20 longitudinal straight ridges were observed on the myxospore surface. The suture line was straight and distinctive, running near the middle of the valves. Histologically, the plasmodia of the present species were found in the Bowman’s capsules, and rarely in the interstitium of the host. Phylogenetic analysis revealed that M. cf. rhodei was sister to M. anatidum in the Myxidium clade including most Myxidium species from freshwater hosts.

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