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In vertebrate animals, especially in fish, collagen has re cently received increased attention as one of the most im portant proteins for the expression of meat texture. Fish meat becomes tender and loses firmness during chilled storage. It has been suggested that this phenomenon of meat tenderization is due to the disintegration of collagen fibers which is caused by an enzymatic degradation, prob ably by the endogenous proteolytic enzymes, of a specific molecular species of collagen, Type V.1-6) This enzymatic degradation of Type V collagen has been suggested by the increased solubility of Type V collagen during chilled storage of fish meat.5,6) In invertebrate animals, however, only limited information is available concerning the contri bution of collagen to meat texture, on abalone,7,8) turban shell,9) and several species of crustacean.10) We previously reported the biochemical characteristics of two genetically distinct types of collagen, named Type SQ-I and SQ-‡U collagens, from the mantle muscle and skin of the squid Todarodes pacificus for the purpose of clarifying the contribution of each molecular species of col lagen to meat texture.11,12) For this purpose, it seems to be very important to localize each collagen type in muscular tissues. In this context, the present study was designed to prepare the antisera against distinct molecular species of collagen, and examine the immunological properties of these antisera, aiming at an application for immuno

Immunochemical Identification of Distinct Molecular Species of Collagen in the Squid Muscle and Skin