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1. Two anionic isoenzymes of glutathione transferases (EC 2.5.1.18), QI and QII, have been purified from the eyes of the shrimp Penaeus japonicus by using a combination of S-hexylglutathione affinity column chromatography and Mono-Q fast protein liquid chromatography (f.p.l.c.). 2. Both QI and II glutathione S-transferases are homodimers. They show(More)
  • N N Chuang
  • Comparative biochemistry and physiology. B…
  • 1990
1. A heat-stable alkaline phosphatase was purified from Penaeus japonicus, with a final specific activity of 21,280 U/mg of protein. 2. In polyacrylamide-gel electrophoresis under non-denaturing conditions, the purified shrimp alkaline phosphatase was found to have an identical molecular size and surface charge as the human placental enzyme. 3. By using(More)
Syndecan-2 was found to detach from RACK1 and associate with caveolin-2 and Ras in cells transformed with oncogenic ras. Most of syndecan-2 from transformed cells was revealed with negligible phosphorylations at tyrosine residues. We experimented with HeLa cells transfected with plasmids encoding syndecan-2 and its mutants (syndecan-2(Y180F),(More)
BALB/3T3 cells were transformed by transfection with DNA encoding the mutated ras(Q(61)K) from shrimp Penaeus japonicus (Huang et al., 2001. J. Exp. Zool. 289:441-448). On a Western blot, the kinase suppressor of Ras (KSR) in the membrane fraction was expressed at slightly reduced level as compared to that of the untransformed cells. To understand this in(More)
Alkaline phosphatase purified from the hepatopancreas of Penaeus japonicus is stable to heating at 65 degree C for 5 min. The specific activity of the purified enzyme is 25,000 units/mg of protein. After polyacrylamide gel electrophoresis under denaturing conditions, the purified alkaline phosphatase from shrimp was found to consist of deglycosylated(More)
A cDNA was isolated from the shrimp Penaeus japonicus by homology cloning. Similar to the mammalian Ras proteins, this shrimp hepatopancreas cDNA encodes a 187-residue polypeptide whose predicted amino acid sequence shares 85% homology with mammalian KB-Ras proteins and demonstrates identity in the guanine nucleotide binding domains. Expression of the cDNA(More)
Receptors for activated C kinase (RACKs) are a group of protein kinase C (PKC) binding proteins that have been shown to be crucial in the translocation and subsequent functioning of PKC on activation. RACK1 isolated from BALB/3T3 cells transformed with S-ras(Q61K) exhibits receptor activity for PKCgamma as competent as that of RACK1 from BALB/3T3 cells(More)
  • N N Chuang
  • Clinica chimica acta; international journal of…
  • 1987
Alkaline phosphatase in human milk was found to be heat stable and have a molecular size of placental alkaline phosphatase, a Mr of 160,000. However, the milk alkaline phosphatase is different from placental alkaline phosphatase. The alkaline phosphatase from milk was endowed with higher surface charge and not inhibited by L-phenylalanine (2.5 mmol/l) and(More)
DNA topoisomerase I was partially purified from the hepatopancreas of the shrimp Penaeus japonicus. The specific activity of the final preparation was 7,000,000 units/mg of protein with SV40 viral DNA as substrate. SDD-polyacrylamide gel electrophoresis of the final preparation yielded two major bands of proteins with M(r) 70,000 and M(r) 67,000, as well as(More)
Phosphotyrosyl protein phosphatase, purified from the hepatopancreas of Panaeus japonicus, is a monomeric enzyme with a relative mass (Mr) of 28,000, as estimated by size-exclusion FPLC on a Superose 12. It has a hydrophobic domain and can be extracted with the detergent CHAPS.The specific activity of the purified enzyme was 9,800 units/mg of protein. The(More)