FERMENTATION OF AT III PRODUCING BHK CELLS IN A DOUBLE MEMBRANE PERFUSION BIOREAKTOR; some aspects about fermentation strategy and process optimization

1991 ◽  
pp. 445-450
Author(s):  
Shu-ying Li ◽  
Bettina Röder ◽  
Manfred Wirth
Keyword(s):  
Process Optimization ◽  
Double Membrane ◽  
Bhk Cells ◽  
At Iii ◽  
Fermentation Strategy

Ultrastructure of Plant Leaf Tissue Infected with Mite-Borne Viral-Like Pathogens

1970 ◽  
Vol 28 ◽  
pp. 178-179 ◽  
Author(s):  
O. E. Bradfute ◽  
R. E. Whitmoyer ◽  
L. R. Nault
Keyword(s):  
Triticum Aestivum ◽  
Zea Mays ◽  
Electron Microscope ◽  
Hordeum Vulgare ◽  
Microscope Study ◽  
Electron Microscope Study ◽  
Leaf Tissue ◽  
Leaf Ultrastructure ◽  
Double Membrane ◽  
Aceria Tulipae

A pathogen transmitted by the eriophyid mite, Aceria tulipae, infects a number of Gramineae producing symptoms similar to wheat spot mosaic virus (1). An electron microscope study of leaf ultrastructure from systemically infected Zea mays, Hordeum vulgare, and Triticum aestivum showed the presence of ovoid, double membrane bodies (0.1 - 0.2 microns) in the cytoplasm of parenchyma, phloem and epidermis cells (Fig. 1 ).

The ultrastructure of the double membrane-bound bodies and endoplasmic reticulum in serial sections of wheat spot mosaic-affected wheat plants

1990 ◽  
Vol 48 (3) ◽  
pp. 694-695
Author(s):  
M. H. Chen ◽  
C. Hiruki
Keyword(s):  
Endoplasmic Reticulum ◽  
High Resolution ◽  
Membrane Structure ◽  
Mosaic Disease ◽  
Serial Sections ◽  
Thin Sections ◽  
Double Membrane ◽  
Southern Alberta ◽  
Membrane Bound ◽  
Scanning Em

Wheat spot mosaic disease was first discovered in southern Alberta, Canada, in 1956. A hitherto unidentified disease-causing agent, transmitted by the eriophyid mite, caused chlorosis, stunting and finally severe necrosis resulting in the death of the affected plants. Double membrane-bound bodies (DMBB), 0.1-0.2 μm in diameter were found to be associated with the disease.Young tissues of leaf and root from 4-wk-old infected wheat plants were fixed, dehydrated, and embedded in Spurr’s resin. Serial sections were collected on slot copper grids and stained. The thin sections were then examined with a Hitachi H-7000 TEM at 75 kV. The membrane structure of the DMBBs was studied by numbering them individually and tracing along the sections to see any physical connection with endoplasmic reticulum (ER) membranes. For high resolution scanning EM, a modification of Tanaka’s method was used. The specimens were examined with a Hitachi Model S-570 SEM in its high resolution mode at 20 kV.

Portein-gold labelling of ultrathin sections of wheat spot mosaic-affected wheat plants

1990 ◽  
Vol 48 (3) ◽  
pp. 680-681
Author(s):  
K. S. Zaychuk ◽  
M. H. Chen ◽  
C. Hiruki
Keyword(s):  
Osmium Tetroxide ◽  
Rnase A ◽  
Leaf Ultrastructure ◽  
Double Membrane ◽  
Young Root ◽  
Leaf Tissues ◽  
Membrane Bound ◽  
Ultrathin Sections ◽  
Gold Labelling ◽  
Electron Dense Core

Wheat spot mosaic (WSpM), which frequently occurs with wheat streak mosaic virus was first reported in 1956 from Alberta. Singly isolated, WSpM causes chlorotic spots, chlorosis, stunting, and sometimes death of the wheat plants. The vector responsible for transmission is the eriophyid mite, Eriophyes tulipae Kiefer. The examination of leaf ultrastructure by electron microscopy has revealed double membrane bound bodies (DMBB’s) 0.1-0.2 μm in diameter. Dispersed fibrils within these bodies suggested the presence of nucleic acid. However, neither ribosomes characteristic of bacteria, mycoplasma and the psittacosis group of organisms nor an electron dense core characteristic of many viruses was commonly evident.In an attempt to determine if the DMBB’s contain nucleic acids, RNase A, DNase I, and lactoferrin protein were conjugated with 10 nm colloidal gold as previously described. Young root and leaf tissues from WSpM-affected wheat plants were fixed in glutaraldehyde, postfixed in osmium tetroxide,and embedded in Spurr’s resin.

Gerinnungsstörungen und Schlaganfall

2006 ◽  
Vol 26 (04) ◽  
pp. 309-315 ◽  
Author(s):  
Ch. C. Eschenfelder ◽  
R. Stingele ◽  
J. A. Zeller
Keyword(s):  
Protein C ◽  
Foramen Ovale ◽  
Offenes Foramen Ovale ◽  
At Iii

ZusammenfassungHereditäre und erworbene Gerinnungsstörungen können bei der Schlaganfallentstehung eine wichtige Rolle spielen. Wegen der Seltenheit der meisten erblichen Gerinnungsstörungen und der erheblichen Kosten, die sich aus einer unkritischen Indikationsstellung ergeben, ist eine maßgeschneiderte Diagnostik sinnvoll. Suggestive Hinweise auf eine Gerinnungsstörung sind niedriges Lebensalter, mehrfache Thrombosen in der Anamnese, altersuntypische Gefäßdegenerationen, vorherige Aborte bei Schlaganfallpatientinnen oder strukturelle Herzveränderungen (z. B. offenes Foramen ovale). Störungen von AT III, Protein C und S, APC-Resistenz, Prothrombinmutation, Homocysteinämie, Antiphospholipidantikörper und prokoagulatorische zelluläre Interaktionen werden diskuiert.

Molekularbiologische Grundlagen und Diagnostik der hereditären Defekte von Antithrombin III, Protein C und Protein S

2002 ◽  
Vol 22 (02) ◽  
pp. 57-66
Author(s):  
I. Witt
Keyword(s):  
Protein C ◽  
Antithrombin Iii ◽  
Protein S ◽  
Klinische Relevanz ◽  
At Iii

ZusammenfassungDie enormen Fortschritte in der Molekularbiologie in den letzten Jahren ermöglichten sowohl die Aufklärung der Nukleotidsequenzen der Gene für Antithrombin III (AT III), Protein C (PROC) und Protein S (PROS) als auch die Identifizierung zahlreicher Mutationen bei hereditären Defekten dieser wichtigen Inhibitoren des plasmatischen Gerinnungssystems. Da die Gene für AT III (13,8 kb) und PROC (11,2 kb) nicht groß und relativ leicht zu analysieren sind, gibt es bereits umfangreiche »databases« der Mutationen (50, 73). Für AT III sind 79 und für PROC 160 unterschiedliche Mutationen beschrieben.Sowohl beim AT-III-Mangel als auch beim Protein-C-Mangel hat die Mutationsaufklärung neue Erkenntnisse über die Struktur-Funktions-Beziehung der Proteine gebracht. Beim Protein-C-Mangel steht die klinische Relevanz der DNA-Analyse im Vordergrund, da die Diagnostik des Protein-C-Mangels auf der Proteinebene nicht immer zuverlässig möglich ist.Das Protein-S-Gen ist für die Analytik schwer zugänglich, da es groß ist (80 kb) und außerdem ein Pseudogen existiert. Es sind schon zahlreiche Mutationen bei Patienten mit Protein-S-Mangel identifiziert worden. Eine Database ist bisher nicht publiziert. Die klinische Notwendigkeit zur Mutationsaufklärung besteht ebenso wie beim Protein-C-Mangel. Es ist zu erwarten, dass zukünftig die Identifizierung von Mutationen auch beim Protein-S-Mangel beschleunigt vorangeht.

Immunologic Studies of Antithrombin III Heparin Cofactor in the Newborn

1978 ◽  
Vol 39 (03) ◽  
pp. 624-630 ◽  
Author(s):  
W E Hathaway ◽  
L L Neumann ◽  
C A Borden ◽  
L J Jacobson
Keyword(s):  
Gestational Age ◽  
Antithrombin Iii ◽  
Newborn Infants ◽  
Term Infant ◽  
Sick Newborn ◽  
At Iii ◽  
Thrombotic Complications ◽  
Low Levels ◽  
Collection Methods ◽  
Made In

SummarySerial quantitative immunoelectrophoretic (IE) measurements of antithrombin III heparin cofactor (AT III) were made in groups of well and sick newborn infants classified by gestational age. Collection methods (venous vs. capillary) did not influence the results; serum IE measurements were comparable to AT III activity by a clotting method. AT III is gestational age-dependent, increasing from 28.7% of normal adult values at 28-32 weeks to 50.9% at 37-40 weeks, and shows a gradual increase to term infant levels (57.4%) by 3-4 weeks of age. Infants with the respiratory distress syndrome (RDS) show lower levels of AT III in the 33-36 week group, 22% vs. 44% and in the 37-40 week group, 33.6% vs. 50.9%, than prematures without RDS. Infants of 28-32 week gestational age had only slight differences, RDS = 24%, non-RDS = 28.7%. The lowest levels of AT III were seen in patients with RDS complicated by disseminated intravascular coagulation and those with necrotizing enterocolitis. Crossed IE on representative infants displayed a consistent pattern which was identical to adult controls except for appropriate decreases in the amplitude of the peaks. The thrombotic complications seen in the sick preterm infant may be related to the low levels of AT III.

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