The casein aggregates cross-linked by micellar calcium phosphate (MCP) were sepatated from goat casein micelles by high performance gel chromatography on a TSK-GEL G4000SW column using 6M urea-simulated milk ultrafiltrate as the eluent. The contents of the casein aggregates cross-linked by MCP were 59.9 and 65.6 % of Saanen and Tokara (Japanese native) goat casein micelles, respectively. These values were higher than those of Holstein cow casein micelles. The high content of the casein aggregates cross-linked by MCP in goat casein micelles is considered to be ascribable to the high content of MCP per casein.

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　On the basis of the result from survey of the activity of intracellular proteinase in Lactococcus lactis subsp. lactis IAM 1198, one of the major caseinolytic proteinases (LLP-II C₂), was purified. Behavior of LLP-II C₂ during cheese ripening was investigated by an immunochemical analysis. Rabbit antiserum against LLP-II C₂ was prepared and the immunochemical relationship between LLP-II C₂ and proteinases in other lactic acid bacteria or commercial cheeses were investigated by the method of Ouchterlony and ELISA. On Ouchterlony gel diffusion test, the antiserum gave a precipitin line against each proteinase II in lactic acid bacteria or cheeses. The reactivity (ELISA value (Absorbance at 405 nm)) between the antiserum and the proteinase of the Gouda type cheese increased gradually for up to 2 months on ripening.

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