TY - JOUR
T1 - Enzymatic and envelope-converting activities of pars recta oviductal fluid from Xenopus laevis
AU - Bakos, Mary Ann
AU - Kurosky, Alexander
AU - Hedrick, Jerry L.
N1 - Funding Information:
This work was supported by NIH Grant CA USPHS Research Grant HD-4906 (J.L.H.).
PY - 1990/3
Y1 - 1990/3
N2 - Conversion of the coelomic egg envelope to the vitelline envelope of the Xenopus laevis egg is known to take place in the pars recta (PR) region of the oviduct. A method for collecting fluid generated from PR cultured in vitro was devised which enhanced the recovery of envelope-converting factors. By the criteria of melting temperature analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, 125I labeling, ferritin binding, and in vitro fertilization assays, the secretions collected from PR cultured in vitro were capable of modifying the envelope in a manner analogous to that which occurred in vivo, including the limited hydrolysis of one envelope glycoprotein. Hydrolytic activities present in PR fluid were assayed with a number of peptide and carbohydrate substrates. Enzymes which hydrolyzed t-butyloxycarbonyl-Leu-Ser-Thr-Arg-methylcouma t-butyloxycarbonyl-Phe-Ser-Arg-methylcoumarylamide, and t-butyloxycarbonyl-Val-Leu-Lys-methylcoumarylamide were found to be present in PR fluid at levels elevated by threefold or more over amounts found in a comparable volume of blood plasma.
AB - Conversion of the coelomic egg envelope to the vitelline envelope of the Xenopus laevis egg is known to take place in the pars recta (PR) region of the oviduct. A method for collecting fluid generated from PR cultured in vitro was devised which enhanced the recovery of envelope-converting factors. By the criteria of melting temperature analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, 125I labeling, ferritin binding, and in vitro fertilization assays, the secretions collected from PR cultured in vitro were capable of modifying the envelope in a manner analogous to that which occurred in vivo, including the limited hydrolysis of one envelope glycoprotein. Hydrolytic activities present in PR fluid were assayed with a number of peptide and carbohydrate substrates. Enzymes which hydrolyzed t-butyloxycarbonyl-Leu-Ser-Thr-Arg-methylcouma t-butyloxycarbonyl-Phe-Ser-Arg-methylcoumarylamide, and t-butyloxycarbonyl-Val-Leu-Lys-methylcoumarylamide were found to be present in PR fluid at levels elevated by threefold or more over amounts found in a comparable volume of blood plasma.
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U2 - 10.1016/0012-1606(90)90186-M
DO - 10.1016/0012-1606(90)90186-M
M3 - Article
C2 - 2307282
AN - SCOPUS:0025195001
SN - 0012-1606
VL - 138
SP - 169
EP - 176
JO - Developmental Biology
JF - Developmental Biology
IS - 1
ER -