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A diverse range of proteins can assemble into amyloid fibrils, a process that generally results in a loss of function and an increase in toxicity. The occurrence and rate of conversion is strongly dependent on several factors including molecular structure and exposure to hydrodynamic forces. To investigate the origins of shear-induced enhancement in the rate of fibrillization, a stable rotating Couette flow was used to evaluate the kinetics of amyloid formation under uniform shear for two similar insulin species (human and bovine) that demonstrate unique fibrillization kinetics. The presence of shear-induced nuclei predicted by previous studies is supported by observations of a lag between the consumption of soluble insulin and the precipitation of amyloid aggregates. The apparent fibrillization rate generally increases with shear. However, a two-parameter kinetic model revealed that the nucleation rate has a maximum value at intermediate shear rates. The fibril elongation rate increases monotonically with shear and is similar for both insulin variants, suggesting that increased elongation rates are related to mixing. Differences between human and bovine insulin kinetics under shear are attributable to the nucleation step.