Abstract
In SDS-electrophoretic analysis of gelatin, much shorter running time and better resolution compared with the standard system have been obtained by using a minislab system. The electrophoretic patterns have clearly shown the characteristics of each gelatin type. In particular, ratios of α-band intensities, αl/α2 of several lime processed gelatins have been examined. The ratios for hide gelatins were larger than 1.5 whereas those for bone gelatins were smaller than 1.1. It is assumed that the deviations from the theoretical ratio for type I collagen could be due to preferential extraction of α2 chains from raw materials.
Notes
Paper presented at the Autumn Meeting organized by the Society of Photographic Science and Technology of Japan, Kyoto, November, 1986.