• Title/Summary/Keyword: orbitally stable

Search Result 3, Processing Time 0.018 seconds

A DELAY-DIFFERENTIAL EQUATION MODEL OF HIV INFECTION OF CD4+ T-CELLS

  • SONG, XINYU;CHENG, SHUHAN
    • Journal of the Korean Mathematical Society
    • /
    • v.42 no.5
    • /
    • pp.1071-1086
    • /
    • 2005
  • In this paper, we introduce a discrete time to the model to describe the time between infection of a CD4$^{+}$ T-cells, and the emission of viral particles on a cellular level. We study the effect of the time delay on the stability of the endemically infected equilibrium, criteria are given to ensure that the infected equilibrium is asymptotically stable for all delay. We also obtain the condition for existence of an orbitally asymptotically stable periodic solution.

DISSIPATIVE RANDOM DYNAMICAL SYSTEMS AND LEVINSON CENTER

  • Asmahan A. Yasir;Ihsan J. Kadhim
    • Nonlinear Functional Analysis and Applications
    • /
    • v.28 no.2
    • /
    • pp.521-535
    • /
    • 2023
  • In this work, some various types of Dissipativity in random dynamical systems are introduced and studied: point, compact, local, bounded and weak. Moreover, the notion of random Levinson center for compactly dissipative random dynamical systems presented and prove some essential results related with this notion.

Combined TGE-SGE Expression of Novel PAI-1-Resistant t-PA in CHO DG44 Cells Using Orbitally Shaking Disposable Bioreactors

  • Davami, Fatemeh;Barkhordari, Farzaneh;Alebouyeh, Mahmoud;Adeli, Ahmad;Mahboudi, Fereidoun
    • Journal of Microbiology and Biotechnology
    • /
    • v.21 no.12
    • /
    • pp.1299-1305
    • /
    • 2011
  • An important modification of thrombolytic agents is resistance to plasminogen activator inhibitor-1 (PAI-1). In previous studies, a new truncated PAI-1-resistant variant was developed based on deletion of the first three domains in t-PA and the substitution of KHRR 128-131 amino acids with AAAA in the truncated t-PA. The novel variant expressed in a static culture system of Chinese Hamster Ovary (CHO) DG44 cells exhibited a higher resistance to PAI-1 when compared with the full-length commercial drug; Actylase. In the present study, the truncated-mutant protein was expressed in CHO DG44 cells in 50 ml orbital shaking bioreactors. The final yield of the truncated-mutant in the culture was 752 IU/ml, representing a 63% increase compared with the static culture system. Therefore, these results suggest that using the combined features of a transient and stable expression system is feasible for the production of novel recombinant proteins in the quantities needed for preclinical studies.