Results 261 to 270 of about 333,295 (341)

Mechanism and modification of rejection of heterografts between divergent species. [PDF]

, 1970
Amemiya, H, Boehmig, HJ, Coburg, AJ, Dixon, FJ, Giles, GR, Hathaway, WE, Lilly, J, Starzl, TE, Takagi, H, Wilson, CB   +9 more
core  

Safety evaluation of the food enzyme thermomycolin from the genetically modified Trichoderma reesei strain AR‐201

EFSA Journal, Volume 23, Issue 10, October 2025.
Abstract The food enzyme thermomycolin (EC 3.4.21.65) is produced with the genetically modified Trichoderma reesei strain AR‐201 by AB Enzymes GmbH. The genetic modifications do not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Henk Van Loveren, Laurence Vernis, Ana Gomes, Magdalena Andryszkiewicz, Daniele Cavanna, Natália Kovalkovičová, Silvia Peluso, Yi Liu   +18 more
wiley   +1 more source

Safety evaluation of the food enzyme chymosin from the genetically modified Trichoderma reesei strain DP‐Nyj88

EFSA Journal, Volume 23, Issue 10, October 2025.
Abstract The food enzyme chymosin (EC 3.4.23.4) is produced with the genetically modified Trichoderma reesei strain DP‐Nyj88 by Genencor International BV. The genetic modifications do not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Henk Van Loveren, Laurence Vernis, Ana Criado, Cristina Fernàndez‐Fraguas, Silvia Peluso, Yi Liu   +16 more
wiley   +1 more source

Safety evaluation of the food enzyme cellulase from the non‐genetically modified Aspergillus niger strain AC 4‐984

EFSA Journal, Volume 23, Issue 10, October 2025.
Abstract The food enzyme cellulase (4‐(1,3;1,4)‐β‐d‐glucan 4‐glucanohydrolase; EC 3.2.1.4) is produced with the non‐genetically modified Aspergillus niger strain AC 4‐984 by Shin Nihon Chemical Co., Ltd. The food enzyme was considered free from viable cells of the production organism.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L.M. Solano, Henk Van Loveren, Laurence Vernis, Magdalena Andryszkiewicz, Daniele Cavanna, Natalia Kovalkovicova, Yi Liu   +16 more
wiley   +1 more source

Development and Validation of a Liquid Chromatography High‐Resolution Mass Spectrometry Method for Blood Desmopressin Quantification and Its Application in Hemophilia A Patients

Rapid Communications in Mass Spectrometry, Volume 39, Issue 18, 30 September 2025.
ABSTRACT Desmopressin (DDAVP), which indirectly increases Coagulation Factor VIII concentrations in the blood, is a common treatment for bleeding disorders such as von Willebrand disease or hemophilia A. However, DDAVP exhibits significant variability in response due to interindividual differences in pharmacokinetics.
Sophie Hodin, Jean Escal, Catherine Feliu, Adeline Pontis, Laurie Josset, Adrian Serban, Benoît Guillet, Xavier Delavenne   +7 more
wiley   +1 more source

Risk Factors for Traumatic Lumbar Puncture in Children With ALL

Acta Paediatrica, Volume 114, Issue 10, Page 2713-2715, October 2025.
Sirkku Setänen, Arja Harila, Viola Metsistö, Christoffer Ehrstedt   +3 more
wiley   +1 more source

Pitfalls in Argatroban Monitoring: Heparin Interference With Dilute Thrombin Time Assays

International Journal of Laboratory Hematology, Volume 47, Issue 5, Page 989-991, October 2025.
Agathe Herb, Jordan Wimmer, Laurent Mauvieux, Laurent Sattler   +3 more
wiley   +1 more source

Activated partial thromboplastin time (APTT), partial thromboplastin time (PTT)

Activated partial thromboplastin time (APTT), partial thromboplastin time (PTT)
openaire   +1 more source

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Activated Partial Thromboplastin Time

Methods in molecular biology, 2013
Activated partial thromboplastin time (APTT) is a commonly used coagulation assay that is easy to perform, is affordable, and is therefore performed in most coagulation laboratories, both clinical and research, worldwide. The APTT is based on the principle that in citrated plasma, the addition of a platelet substitute, factor XII activator, and CaCl2 ...
V. Ignjatovic
semanticscholar   +5 more sources

Activated Partial Thromboplastin Time and Prothrombin Time Mixing Studies: Current State of the Art

Seminars in Thrombosis and Hemostasis, 2022
Mixing studies have long been in the clinical laboratory armamentarium for investigating unexpected, prolonged activated partial thromboplastin time (aPTT) or prothrombin time (PT).
D. Adcock, G. Moore, S. Montalvão, G. Kershaw, R. Gosselin   +4 more
semanticscholar   +1 more source