Zobrazeno 1 - 10
of 30
pro vyhledávání: '"C M Ketcham"'
Autor:
Stuart Kornfeld, C M Ketcham
Publikováno v:
Journal of Biological Chemistry. 267:11654-11659
The kinetic properties of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase (GlcNAc-phosphotransferase) partially purified from the soil amoeba Acanthamoeba castellanii have been studied. The transferase phosphorylated the
Autor:
Stuart Kornfeld, C M Ketcham
Publikováno v:
Journal of Biological Chemistry. 267:11645-11653
UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase (GlcNAc-phosphotransferase) from the soil amoeba Acanthamoeba castellanii has been purified over 100,000-fold by means of wheat germ agglutinin-Sepharose affinity chromatog
Publikováno v:
The Journal of Cell Biology
Scopus-Elsevier
Scopus-Elsevier
A procedure has been established in Vero cells for the isolation of an intermediate compartment involved in protein transport from the ER to the Golgi apparatus. The two-step subcellular fractionation procedure consists of Percoll followed by Metriza
Autor:
C M, Ketcham, S, Kornfeld
Publikováno v:
The Journal of biological chemistry. 267(16)
The kinetic properties of UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase (GlcNAc-phosphotransferase) partially purified from the soil amoeba Acanthamoeba castellanii have been studied. The transferase phosphorylated the
Autor:
C M, Ketcham, S, Kornfeld
Publikováno v:
The Journal of biological chemistry. 267(16)
UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase (GlcNAc-phosphotransferase) from the soil amoeba Acanthamoeba castellanii has been purified over 100,000-fold by means of wheat germ agglutinin-Sepharose affinity chromatog
Publikováno v:
The Journal of biological chemistry. 261(27)
A pink, high molecular weight form of uteroferrin (Uf) has been isolated from uterine secretions and allantoic fluid of pigs. This protein fraction (denoted FIII) which is relatively stable under physiological conditions of pH, ionic strength, and te
Publikováno v:
Advances in experimental medicine and biology. 230
The uterus of the pig secretes large amounts of protein in response to progesterone. Estrogen alone has little effect but in combination with progesterone is synergistic at low doses and inhibitory at high doses. The responses of the uterus to proges
Publikováno v:
The Journal of biological chemistry. 260(9)
The spleens of patients with hairy cell leukemia contain high levels of a tartrate-insensitive, cationic, acid phosphatase (the human Type 5 isozyme). This phosphatase has been purified by a procedure which involves only two chromatographic steps: CM
Publikováno v:
The Journal of biological chemistry. 264(1)
The type 5, iron-containing, tartrate-resistant acid phosphatase (TR-AP) constitutes a relatively minor intracellular isozyme of acid phosphatase in the human that is immunologically related to uteroferrin, a secreted progesterone-induced protein of
Autor:
Nishimura T; Faculty of Pharmacy, Keio University, 1-5-30 Shibakoen, 105-8512, Minato-ku, Tokyo, Japan., Shiga K; Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba, 980-8578, Aramaki, Aoba-ku, Sendai, Japan., Sekiya M; Division of Biochemistry, School of Pharmacy, Iwate Medical University, 1-1-1 Idaidori, 028-3694, Yahaba-cho, Shiwa-gun, Iwate, Japan., Sugawara A; Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba, 980-8578, Aramaki, Aoba-ku, Sendai, Japan.; Present address: Ōmura Satoshi Memorial Institute, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo, 108-8641, Japan., Yonezawa T; Research Institute for Biological Functions, Chubu University, 1200 Matsumoto-cho, 487-8501, Kasugai, Aichi, Japan., Kikuchi H; Faculty of Pharmacy, Keio University, 1-5-30 Shibakoen, 105-8512, Minato-ku, Tokyo, Japan.; Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba, 980-8578, Aramaki, Aoba-ku, Sendai, Japan.
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Aug 27; Vol. 30 (48), pp. e202402082. Date of Electronic Publication: 2024 Aug 02.