Purpose: To evaluate the effects of proteoglycan and type II collagen within articular cartilage on T1ρ relaxation time of articular cartilage. Materials and Methods: This study was exempted by the institutional and animal review boards, and informed consent was not required. Twelve porcine patellae were assigned to three groups of control, trypsin-treated (proteoglycan-degraded), or collagenase-treated (collagen-degraded). The T1ρ images were obtained with a 3 tesla magnetic resonance imaging scanner with a single loop coil. Statistical differences were detected by analysis of variance to evaluate the effects of the enzyme on T1ρ relaxation time. Safranin-O was used to stain proteoglycan in the articular cartilage and immunohistochemical staining was performed for type II collagen. Results: Mean T1ρ values of the control, trypsin-treated, and collagenase-treated groups were 37.72 ± 5.82, 57.53 ± 8.24, and 45.08 ± 5.31 msec, respectively ( p < 0.001). Histology confirmed a loss of proteoglycan and type II collagen in the trypsin- and collagenase-treated groups. Conclusion: Degradation of proteoglycans and collagen fibers in the articular cartilage increased the articular cartilage T1ρ value.