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- W2000599726 abstract "The dynamic, steady-shear and transient shear flow properties of precisely prepared link-stable (s0 136, 66% aggregate) and link-free (s0 93, 59% aggregate) proteoglycan aggregate solutions at concentrations ranging from 10 to 50 mg/ml were determined using a cone-on-plate viscometer in a mechanical spectrometer. All proteoglycan solutions tested possessed: (1) linear viscoelastic properties — as measured by the dynamic complex modulus under small amplitude steady oscillatory conditions (1 ≤ ω ≤ 100 rad/s) — and (2) nonlinear shear-rate dependent apparent viscosities and primary normal stress difference under steady shearing conditions (0.25 ≤ γ̇ ≤ 250 s−1). Our transient flow data show that all proteoglycan aggregate solutions exhibited transient stress overshoot effects in shear stress and normal stress. From these steady and transient flow data, we conclude that link protein stabilized aggregates have significant effects on their dynamic and steady-shear properties as well as transient flow properties. The transient stress overshoot data provide a measure of the energy per unit volume of fluid required to overcome the proteoglycan networks in solution from a resting state. Thus we found that link-stable aggregates form much stronger networks than link-free aggregates. This is corroborated by the fact that link-stable aggregates form more elastic (lower tan δ) and stiffer (higher ⋎G∗|) networks than link-free aggregates. The complete spectrum of viscometric flow data is entirely compatible with the proposed role of link protein in adding structural stability to the proteoglycan-hyaluronate bond. In cartilage, the enhanced strength of the networks formed by link-stable aggregates may play an important role in determining the material properties of the tissue and thereby contribute to the functional capacity of cartilage in diarthrodial joints." @default.
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- W2000599726 date "1989-08-01" @default.
- W2000599726 modified "2023-10-14" @default.
- W2000599726 title "The influence of link protein stabilization on the viscometric properties of proteoglycan aggregate solutions" @default.
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- W2000599726 doi "https://doi.org/10.1016/0304-4165(89)90011-1" @default.
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