IntroductionTenecteplase (TNK), a novel genetically modified variant of tissue-type plasminogen activator (rt-PA), holds great promise as a first-line thrombolytic agent for thrombotic diseases owing to its convenient administration and favorable pharmacological properties. However, glycosylation heterogeneity derived from distinct production processes has resulted in industry-wide inconsistencies in enzyme activity determination methods, reference materials, and activity units, severely impairi
Core determinant of the in vitro enzyme activity of tenecteplase: primary structure over glycosylation modifications
Jing Li
