Differentiation- and apoptosis-inducing activities by pentacyclic triterpenes on a mouse melanoma cell line.

In a study to investigate the relationship between the chemical structure and the differentiation-inducing activity of pentacyclic triterpenes, several lupane, oleanane, and ursane triterpenes were prepared and their effects on B16 2F2 melanoma cell differentiation and growth were examined. Eleven lupane triterpenes used in this study acted on the melanoma cells as a melanogen, but no induction of melanogenesis of B16 2F2 cells by oleanane and ursane was detected. The differences at C-17 of the lupane series and acetylation of the OH group at C-3 did not markedly influence their activities.

Identification of a domain conferring nucleotide binding to the N-acetyl-d-glucosamine 2-epimerase (Renin binding protein).

Renin binding protein (RnBP), a cellular renin inhibitor, has been identified as the enzyme N-acetyl-D-glucosamine (GlcNAc) 2-epimerase. Our recent studies demonstrated that rat GlcNAc 2-epimerase has a ten-times higher affinity for ATP, dATP, and ddATP than the human enzyme [Takahashi, S. et al.

Effects of nucleotides on N-acetyl-d-glucosamine 2-epimerases (renin-binding proteins): comparative biochemical studies.

Renin-binding protein (RnBP) is an endogenous renin inhibitor originally isolated from porcine kidney as a complex of renin, so-called high molecular weight (HMW) renin. Our recent studies demonstrated that human RnBP is the enzyme N-acetyl-D-glucosamine (GlcNAc) 2-epimerase [Takahashi, S. et al.

Molecular cloning of acid-stable glucose isomerase gene from Streptomyces olivaceoviridis E-86 by a simple two-step PCR method, and its expression in Escherichia coli.

Glucose isomerase (GI) from Streptomyces olivaceoviridis E-86 is a unique enzyme, very acid-stable with a large potential for corn sweetener industries. The gene encoding this unique enzyme was cloned by a simple two-step PCR method, and expressed in Escherichia coli. A single open reading frame consisting of 1164 base pairs (70.

Identification of functionally important cysteine residues of the human renin-binding protein as the enzyme N-acetyl-D-glucosamine 2-epimerase.

Renin-binding protein (RnBP) is an endogenous renin inhibitor originally isolated from porcine kidney. It was recently identified as the enzyme N-acetyl-D-glucosamine (GlcNAc) 2-epimerase [Takahashi, S. et al.

Renin inhibits N-acetyl-D-glucosamine 2-epimerase (renin-binding protein).

Renin-binding protein (RnBP) is a highly specific renin inhibitor first isolated from porcine kidney. Our recent studies demonstrated that the human RnBP is the enzyme N-acetyl-D-glucosamine (GlcNAc) 2-epimerase [Takahashi, S. et al.

Differentiation-inducing activity of lupeol, a lupane-type triterpene from Chinese dandelion root (Hokouei-kon), on a mouse melanoma cell line.

We examined the differentiation-inducing effects of extracts of 49 wild plants, 25 types of seaweed and 26 mushrooms in Akita on the human leukemia cell line HL60 and a B16 mouse melanoma-derived sub-clone with high differentiation capability (B16 2F2). Differentiation inducers of HL60 cells such as retinoic acid, showed no effects on the differentiation of B16 2F2 cells. Furthermore, chemical compounds known to be inducers of B16 cells, did not induce differentiation of HL60 cells.

Characterization of acid-stable glucose isomerase from Streptomyces sp., and development of single-step processes for high-fructose corn sweetener (HFCS) production.

The glucose isomerase from Streptomyces olivaceoviridis E-86 was purified by chromatographic procedures, showing one single protein band in the SDS-PAGE. The enzyme had high acid stability, and there was no loss in enzyme activity at pH 5.0 after incubation at 60 degrees C for 30 hr.

Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein).

Renin binding protein (RnBP) is a proteinous renin inhibitor firstly isolated from porcine kidney. Recently, the protein was identified as the enzyme, N-acetyl-D-glucosamine (GlcNAc) 2-epimerase. The GlcNAc 2-epimerase activity of recombinant human RnBP was specifically inhibited by SH-reagents such as N-ethylmaleimide, 5, 5'-dithiobis-2-nitrobenzoate, and iodoacetic acid, indicating that the most probable reactive site is a cysteine residue.

Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase.

The existence of human renin-binding protein (RnBP) in the kidney has been shown by the isolation and characterization of a complex of porcine renin-human RnBP [S. Takahashi et al. (1985) J.

Substantially Complete Removal of Three Major Allergenic Soybean Proteins (Gly m Bd 30K, Gly m Bd 28K, and the α-Subunit of Conglycinin) from Soy Protein by Using a Mutant Soybean, Tohoku 124.

A wild-type soybean contains three major allergenic proteins, Gly m Bd 30K, the α-subunit of conglycinin, and Gly m Bd 28K. A genetically mutated soybean (Tohoku 124), which was originally developed as a cultivar lacking the α- and α'-subunits of conglycinin, was also found to lack Gly m Bd 28K from immunoblot analysis using monoclonal antibodies specific to Gly m Bd 28K. This finding indicates the possibility to prepare soy milk and soy proteins containing none of the three major allergenic soybean proteins from this cultivar.