[A study of collangenic polypeptide in gallstones and its role in stone formation].
Observations on sections of human gallstone with electron microscope and analysis of glycoprotein extracted from the stone for amino acids and sulfuric rachiles radicals demonstrated that it was sulphatized glycoprotein and that the fibrous strauds of protein might be precollange-collagenic polypeptide. Inflammation was an important factor in the formation of gallstone. Increased and deposited collangenic polypeptide as nuclei with positive charges in the acid circumstances could combine not only with acid polysaccharide with negative charges into glycoprotein, but also with pigment or/and cholesterol stone with negative charges into crystal, and occupied all spaces of the fibroid structure. Deposition of cations such as K+ Na+, Ca++, increased the size of the stone. The authors pointed out that the acid polysaccharide could prevent the collangenic polypeptide from digestion of proteinase. Therefore, weak base should be first used in solution of gallstone to hydrolyze the acid polypeptide.
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D000818:Animals; D002352:Carrier Proteins; D002769:Cholelithiasis / Q000032:analysis / Q000209:etiology* / Q000378:metabolism; D006224:Cricetinae; D005260:Female; D006023:Glycoproteins / Q000032:analysis; D008297:Male; D010455:Peptides / Q000032:analysis; D011506:Proteins / Q000032:analysis*
D002352:Carrier Proteins; D006023:Glycoproteins; D010455:Peptides; D011506:Proteins; C007105:c1q-binding proteins