TY - JOUR
T1 - Isolation and characterization of human placental chorionic villar extracellular matrix
AU - Ohno, M.
AU - Nagle, R. B.
AU - Meezan, E.
AU - Brendel, K.
PY - 1979
Y1 - 1979
N2 - The cell-free extracellular matrix of human placenta chorionic villi has been prepared by a procedure employing extraction of the terminal villar fragments with the detergents. Triton X-100 and sodium deoxycholate. The isolated human placental extracellular matrix retains an intact, but collapsed, histoarchitecture, as observed by scanning and transmission electron microscopy. It remains intact, in large part because of the presence of continous sheets of villar basement membranes and associated interstitial collagen fibers and scattered patches of fibrin. The staining characteristics and chemical composition of the isolated human placental extracellular matrix are similar to those reported for basement membranes in several tissues and indicate the presence of collagen-like and glycoprotein components in this preparation. Gel electrophoresis of urea-SDS-mercaptoethanol extracts of the matrix showed that it consists of several polypeptide components of various molecular weights, some of which are associated into high molecular weight complexes by disulfide bonds.
AB - The cell-free extracellular matrix of human placenta chorionic villi has been prepared by a procedure employing extraction of the terminal villar fragments with the detergents. Triton X-100 and sodium deoxycholate. The isolated human placental extracellular matrix retains an intact, but collapsed, histoarchitecture, as observed by scanning and transmission electron microscopy. It remains intact, in large part because of the presence of continous sheets of villar basement membranes and associated interstitial collagen fibers and scattered patches of fibrin. The staining characteristics and chemical composition of the isolated human placental extracellular matrix are similar to those reported for basement membranes in several tissues and indicate the presence of collagen-like and glycoprotein components in this preparation. Gel electrophoresis of urea-SDS-mercaptoethanol extracts of the matrix showed that it consists of several polypeptide components of various molecular weights, some of which are associated into high molecular weight complexes by disulfide bonds.
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U2 - 10.1002/jss.400120405
DO - 10.1002/jss.400120405
M3 - Article
C2 - 550010
AN - SCOPUS:0018768229
SN - 0730-2312
VL - 12
SP - 457
EP - 466
JO - Journal of Supramolecular and Cellular Biochemistry
JF - Journal of Supramolecular and Cellular Biochemistry
IS - 4
ER -