Abstract
Publisher Summary This chapter discusses purification, specificity and physical properties of the bacterial enzymes and focuses on the use of the enzyme for the analysis and identification of collagen species. Purification of the enzyme and sequence specificity is discussed from the standpoint of obtaining an enzyme preparation free of other proteolytic enzyme activity and capable of quantitatively and specifically digesting collagen in a mixture of proteins. Limited digestion with bacterial collagenases can be used to obtain information on the helical region of collagen. The site of cleavage is determined by electron microscopy of segment long-spacing fragments or Edman degradation. At a low enzyme-to-substrate ratio, cleavage occurred mainly at two sites—interbands 26–27 and 33–34 in calf skin collagen, but at bands 18 and 22 in rat skin collagen. Highly purified A. iophagus collagenase produced cleavages mainly at bands 33-34 and 41 in both types of collagen.
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