Zobrazeno 1 - 7
of 7
pro vyhledávání: '"J L Weickmann"'
Publikováno v:
Journal of Biological Chemistry. 253:6010-6015
Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The S020,w and D020,w values of the enzyme are 5.48 S and 5.87 X 10(-7) cm3/s, re
Autor:
D E Fahrney, J L Weickmann
Publikováno v:
Journal of Biological Chemistry. 252:2615-2620
Arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis ATCC 14152 has been purified 6-fold by a new procedure, protamine sulfate fractionation and DEAE-agarose chromatography. The yield was 75 to 85%. The homogeneity of the final preparation was
Human ribonucleases. Quantitation of pancreatic-like enzymes in serum, urine, and organ preparations
Autor:
D G Glitz, J L Weickmann
Publikováno v:
Journal of Biological Chemistry. 257:8705-8710
Antibodies against pure human pancreatic ribonuclease (RNase) were used to study ribonuclease levels in human tissues and body fluids. The antibodies completely inhibit the activity of purified RNase as well as ribonuclease activity in crude pancreat
Publikováno v:
Cancer research. 44(4)
Serum levels of RNase activity, presumed to originate in the pancreas, have been suggested to be of use in the diagnosis of pancreatic cancer. We have used a radioimmunological assay of human pancreatic-like RNase to quantitate this protein in serum
Human ribonucleases. Quantitation of pancreatic-like enzymes in serum, urine, and organ preparations
Autor:
J L, Weickmann, D G, Glitz
Publikováno v:
The Journal of biological chemistry. 257(15)
Antibodies against pure human pancreatic ribonuclease (RNase) were used to study ribonuclease levels in human tissues and body fluids. The antibodies completely inhibit the activity of purified RNase as well as ribonuclease activity in crude pancreat
Publikováno v:
The Journal of biological chemistry. 253(17)
Hydrodynamic, chemical, and optical properties of arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis are reported for the enzyme isolated from log phase cells. The S020,w and D020,w values of the enzyme are 5.48 S and 5.87 X 10(-7) cm3/s, re
Autor:
J L, Weickmann, D E, Fahrney
Publikováno v:
The Journal of biological chemistry. 252(8)
Arginine deiminase (EC 3.5.3.6) from Mycoplasma arthritidis ATCC 14152 has been purified 6-fold by a new procedure, protamine sulfate fractionation and DEAE-agarose chromatography. The yield was 75 to 85%. The homogeneity of the final preparation was