Binding of human serum proteins to XXXX particles in vitro.

@entity3208 @entity2262 @entity904 @entity2975 @entity6701 @entity3759 @entity214
OBJECTIVES: To determine the capacity of human serum proteins to bind to @entity6701 ( @entity3759 ) particles of different polymorphs and sizes. METHODS: @entity3759 particles were mixed with diluted human serum, purified human serum albumin (HSA) or purified human serum gamma-globulin (HGG) solutions. After incubation at 37  C for 1 h, the particles were sedimented by centrifugation, and proteins in the supernatant, as well as those bound to the particles, were analyzed. RESULTS: The total protein concentration in the supernatant was lowered by @entity3759 , whereas the albumin/globulin ratio was elevated by the particles. Incubation with @entity3759 also lowered the immunoglobulin, pre-albumin, @entity2262 , ceruloplasmin and @entity904 -binding protein levels, but not ferritin levels, in the supernatant. After @entity3208 - @entity2975 gel electrophoresis ( @entity214 -PAGE), proteins in the supernatant, especially HGG, were observed to decrease, while those released from the particles (after adding 1% @entity214 and heating) increased, depending on the dose of @entity3759 . Purified HGG and HSA were also bound to @entity3759 , although the former appeared to have a higher affinity. All the proteins tested showed the highest binding potency to the amorphous particles (<50 nm) and the lowest to the rutile particles (<5,000 nm), while binding to anatase particles was intermediate. The affinity to the larger anatase was higher than that to smaller anatase particles in most cases. CONCLUSIONS: Human serum proteins, including the two major components, HSA and HGG, are bound by @entity3759 particles. The polymorph of the particles seems to be important for determining the binding capacity of the particles and it may affect distribution of the particles in the body.
