Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Sukumar Medda"'
Publikováno v:
Journal of Cellular Biochemistry. 65:11-24
Osteoblasts undergo a temporal sequence of development characterized by transcriptional upregulation of osteoblast-specific genes. Basic helix-loop-helix (bHLH) transcription factors may control this developmental process through binding to E-box cis
Autor:
Richard L. Proia, Sukumar Medda
Publikováno v:
European journal of biochemistry. 206(3)
Resident proteins of the endoplasmic reticulum lumen are continuously retrieved from an early Golgi compartment by a receptor-mediated mechanism. The sorting or retention sequence on the endoplasmic reticulum proteins is located at the C-terminus and
Autor:
Dennis A. Stephenson, Katherine Tepperman, Roger E. Ganschow, Stephen G. Grant, Sukumar Medda, Mariana Ovnic, Rosemary W. Elliott
Publikováno v:
Genomics. 9(2)
We have characterized a mRNA sequence containing the entire coding region of a mouse carboxylesterase (EC 3.1.1.1). pEs-N, an 1840-bp composite of five overlapping cDNA clones, contains an open reading frame of 554 amino acids that display a high deg
Publikováno v:
Journal of Biological Chemistry. 262:7248-7253
We report biochemical, immunological, and genetic studies which demonstrate that an accessory protein with the essential features of mouse egasyn is complexed with and stabilizes a portion of beta-glucuronidase in microsomes of rat liver. The accesso
Autor:
Sukumar Medda, Richard T. Swank
Publikováno v:
Journal of Biological Chemistry. 260:15802-15808
The glycoprotein egasyn complexes with and stabilizes precursor beta-glucuronidase in microsomes of several mouse organs. Several observations indicate egasyn is, in addition, an esterase. Liver homogenates of egasyn-positive strains have specific el
Publikováno v:
Journal of the Faculty of Agriculture, Kyushu University. 26:139-149
Publikováno v:
Biochemical Genetics. 24:229-243
Recent experiments have demonstrated that egasyn not only sequesters beta-glucuronidase in microsomes by forming high molecular weight complexes with beta-glucuronidase, but also has carboxyl esterase activity. We have found several new phenotypes of
Publikováno v:
Journal of Biological Chemistry. 264:15824-15828
The proenzyme form of beta-glucuronidase is compartmentalized in large quantities within the endoplasmic reticulum by binding to the esterase, egasyn. Also, the propeptide of the proenzyme form of beta-glucuronidase is likely located at the carboxyl
Autor:
Eric E. Smith, Sukumar Medda
Publikováno v:
Analytical Biochemistry. 138:354-359
A method has been developed for the assay of amylomaltase based on the incorporation of a [14C]glucose moiety of uniformly 14C-labeled maltose into a maltodextrin fraction insoluble in aqueous ethanol. The presence of dextrin at a high concentration
Publikováno v:
Cell. 50:301-310
Organophosphorous compounds, which are potent inhibitors of egasyn-esterase activity, caused a rapid dissociation of the high molecular weight egasyn-microsomal beta-glucuronidase complex when administered in vivo or when added in vitro to microsomal