Benign prostatic hyperplasia (BPH) is difficult to discriminate from prostate carcinoma (PCa) preoperatively. The non-invasive biomarkers are necessary to reduce the burden of biopsies and improve survival quality of patients. Previous research suggests that abnormal glycosylation of immunoglobulin gamma molecules (IgGs) may associated with immunological diseases and prostate diseases. Hence, characterizing intact N-glycopeptides of IgGs that correspond to N-glycan structure with specific site information enable better understanding of the molecular pathogenesis and finding out some novel signatures in preoperative discrimination of BPH from PCa. In this study, we profiled intact N-glycopeptides of purified IgGs from 51 PCa patients and 45 BPH patients by our developed N-glycoproteomic method using hydrophilic interaction liquid chromatography enrichment coupled with high resolution LC-MS/MS, and intact N-glycopeptides quantitative analysis was performed using pGlyco 2.0 and MaxQuant softwares. Our data provided plasma IgG subclass-specific and site-specific N-glycosylation quantitative information.