Nitrogen stable isotope techniques are widely used in ecology, archaeology and forensic science to explore trophic relationships and provenances of organisms and materials, most widely using bulk δ 15 N values of whole organisms, tissues or other materials. However, compound-specific isotope values can provide more diagnostic isotope "fingerprints" and specific information about metabolic processes. Existing techniques for nitrogen isotope analysis allow the determination of δ 15 N values of 14 amino acids (AAs), accounting for ca. 75% of plant protein and collagen N. The majority of remaining N is from arginine, comprising 16% and 14% of collagen and plant protein N, respectively. We therefore aimed to develop a method to detect arginine and determine its δ 15 N value (δ 15 NArg) by GC-C-IRMS, to further contribute to the understanding of metabolic routing of this important AA. We demonstrate that arginine, as its N-acetyl isopropyl ester, is amenable to GC analysis using a 15 m mid-polarity DB-35 column, eluting with baseline resolution from other AAs. The recorded δ 15 N value by GC-C-IRMS was within error of that of the underivatized compound determined by EA-IRMS. The newly-developed GC-C-IRMS method was applied to modern plant protein and cattle collagen, enabling their δ 15 NArg values to be related to AA biosynthesis. Determinations of archaeological cattle collagen δ 15 NArg values confirmed the suitability of this method to provide further insights into past diets and ecosystems. Bulk collagen δ 15 N value reconstruction including δ 15 NArg values better reflect measured bulk values, as the isotopic ratio of 91‰ of collagen N can now be determined at the compound-specific level.