This study presents a detailed analysis of the molecular weight and structural characteristics of protease inhibitors (PIs) isolated from chickpea (Cicer arietinum). The research employs Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) for primary molecular weight determination and matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry for precise mass analysis and initial structural insights. The results confirm the presence of multiple PI isoforms with molecular weights predominantly in the range of 8-20 kDa, consistent with the Bowman-Birk and Kunitz inhibitor families. These findings provide a foundational proteomic profile crucial for understanding the structure function relationship of chickpea PIs, which have significant implications in plant defense mechanisms and human nutrition.