acebutolol and 4-nitrophenylmaltoside

acebutolol has been researched along with 4-nitrophenylmaltoside in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Nakatani, H; Tonomura, B; Yamashita, H	1
Lanskaya, IM; Lukomskaya, IS; Podkidisheva, EI; Voznyi, YV	1

Other Studies

2 other study(ies) available for acebutolol and 4-nitrophenylmaltoside

Article	Year
Effect of a p-nitro group of phenyl-maltooligosaccharide substrate on the change of action specificity of lysine-modified porcine pancreatic alpha-amylase. Biochemistry and molecular biology international, 1995, Volume: 35, Issue:1 Topics: alpha-Amylases; Animals; Glucose; Glucosides; Kinetics; Lysine; Maltose; Nitrobenzenes; Oligosaccharides; Pancreas; Structure-Activity Relationship; Substrate Specificity; Swine; Trisaccharides	1995
Use of beta-maltosides (p-nitrophenyl-beta-D-maltoside, 2-chloro-4- nitrophenyl-beta-D-maltoside and 4-methylumbelliferyl-beta-D-maltoside) as substrates for the assay of neutral alpha-glucosidase from human kidney and urine. Clinica chimica acta; international journal of clinical chemistry, 1996, Jan-31, Volume: 244, Issue:2 Topics: Acetylglucosaminidase; alpha-Galactosidase; Automation; Glucosides; Humans; Hymecromone; Kidney; Kidney Transplantation; Kinetics; Maltose; Microvilli; Nitrobenzenes; Sensitivity and Specificity; Spectrophotometry; Substrate Specificity	1996

Article

Year

Effect of a p-nitro group of phenyl-maltooligosaccharide substrate on the change of action specificity of lysine-modified porcine pancreatic alpha-amylase.

Biochemistry and molecular biology international, 1995, Volume: 35, Issue:1

Topics: alpha-Amylases; Animals; Glucose; Glucosides; Kinetics; Lysine; Maltose; Nitrobenzenes; Oligosaccharides; Pancreas; Structure-Activity Relationship; Substrate Specificity; Swine; Trisaccharides

1995

Use of beta-maltosides (p-nitrophenyl-beta-D-maltoside, 2-chloro-4- nitrophenyl-beta-D-maltoside and 4-methylumbelliferyl-beta-D-maltoside) as substrates for the assay of neutral alpha-glucosidase from human kidney and urine.

Clinica chimica acta; international journal of clinical chemistry, 1996, Jan-31, Volume: 244, Issue:2

Topics: Acetylglucosaminidase; alpha-Galactosidase; Automation; Glucosides; Humans; Hymecromone; Kidney; Kidney Transplantation; Kinetics; Maltose; Microvilli; Nitrobenzenes; Sensitivity and Specificity; Spectrophotometry; Substrate Specificity

1996