01813nas a2200217   4500008004100000020001400041245007100055210006600126260001500192300001400207490000800221520114400229653002301373653002701396653001301423653001601436100002901452700002201481700002201503856007001525       1981                        eng d  a0005-274400aProperties of a collagenolytic enzyme from <i>Bipalium kewense</i>0 aProperties of a collagenolytic enzyme from iBipalium kewensei  c1981/10/13  a213 - 2200 v6613 a<p>A collagenolytic enzyme from the land planarian Bipalium kewense has been purified by preparative isoelectric focusing. The enzyme has a molecular weight of 47 000 &plusmn; 2 000 and appears to be dimeric. It has an isoelectric point of 4.6 &plusmn; 0.1 and a high content of acidic amino acids. The amino acid composition of the Bipalium collagenase is similar to that of human skin fibroblast collagenases but clearly different from previously reported collagenolytic proteases from other invertebrates, Uca pugilator and Hypoderma lineatum. In its action on guinea-pig collagen, the enzyme produces distinct products, at low incubation temperatures, different from those produced by vertebrate and other invertebrate collagenolytic enzymes. These products have glycine as their N-terminal amino acids. As determined by viscosity measurements, the Bipalium collagenase is more active on invertebrate, earthworm, collagen than it is on the vertebrate, Type I guinea-pig skin, collagen. The Bipalium collagenase differs from both bacterial and vertebrate collagenases as well as from invertebrate, collagenolytic serine proteases.</p>
10a(Bipalium kewense)10aAmino acid composition10aCollagen10aCollagenase1 aLandsperger, William, J.1 aPeters, Erwin, H.1 aDresden, Marc, H.  uhttp://www.sciencedirect.com/science/article/pii/0005274481900061