guanidine has been researched along with acid phosphatase in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 4 (50.00) | 18.2507 |
| 2000's | 3 (37.50) | 29.6817 |
| 2010's | 1 (12.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Dinischiotu, A; Dumitru, IF | 1 |
| Cashikar, AG; Rao, NM | 2 |
| Chen, QX; Chen, SL; Qiu, WJ; Wang, LT; Yang, PZ; Zhou, HM | 1 |
| Bakalova, A; Kuciel, R; Mazurkiewicz, A; Wójciak, P | 1 |
| Aoyama, H; Cavagis, AD; Ferreira, CV; Granjeiro, PA | 1 |
| Dudzik, P; Kuciel, R; Mazurkiewicz, A | 1 |
| Avnir, D; Vinogradov, VV; Volodina, KV | 1 |
8 other study(ies) available for guanidine and acid phosphatase
| Article | Year |
|---|---|
Cock seminal plasma acid phosphatase: active site directed inactivation, crystallization and in vitro denaturation-renaturation studies.
Topics: Acid Phosphatase; Animals; Binding Sites; Chickens; Crystallization; Enzyme Stability; Guanidine; Guanidines; In Vitro Techniques; Iodoacetates; Iodoacetic Acid; Male; Protein Denaturation; Semen; Sulfhydryl Reagents | 1994 |
Unfolding pathway in red kidney bean acid phosphatase is dependent on ligand binding.
Topics: Acid Phosphatase; Adenosine Triphosphate; Circular Dichroism; Fabaceae; Fluorescent Dyes; Guanidine; Guanidines; Kinetics; Ligands; Mercaptoethanol; Phosphates; Plants, Medicinal; Potassium Iodide; Protein Conformation; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Tryptophan | 1996 |
Role of the intersubunit disulfide bond in the unfolding pathway of dimeric red kidney bean purple acid phosphatase.
Topics: Acid Phosphatase; Anilino Naphthalenesulfonates; Chromatography, Gel; Circular Dichroism; Disulfides; Enzyme Stability; Fabaceae; Glycoproteins; Guanidine; Guanidines; Plants, Medicinal; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Tryptophan | 1996 |
Unfolding and inactivation of Penaeus penicillatus acid phosphatase during denaturation by guanidine hydrochloride.
Topics: Acid Phosphatase; Animals; Binding Sites; Circular Dichroism; Guanidine; Guanidines; Penaeidae; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 1997 |
Equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate.
Topics: Acid Phosphatase; Catalysis; Catalytic Domain; Chromatography; Chromatography, High Pressure Liquid; Cysteine; Dimerization; Dose-Response Relationship, Drug; Guanidine; Humans; Kinetics; Male; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Protein Tyrosine Phosphatases; Spectrometry, Fluorescence; Thermodynamics; Time Factors; Tryptophan | 2003 |
Effect of chaotropic agents on reversible unfolding of a soybean (Glycine max) seed acid phosphatase.
Topics: Acid Phosphatase; Glycine max; Guanidine; Protein Denaturation; Protein Folding; Seeds; Spectrometry, Fluorescence; Thermodynamics; Urea | 2004 |
Kinetic intermediates of unfolding of dimeric prostatic phosphatase.
Topics: Acid Phosphatase; Anilino Naphthalenesulfonates; Congo Red; Dimerization; Dithionitrobenzoic Acid; Enzyme Inhibitors; Guanidine; Humans; In Vitro Techniques; Kinetics; Male; Prostate; Protein Denaturation; Protein Folding; Protein Structure, Quaternary; Protein Tyrosine Phosphatases; Spectrometry, Fluorescence; Sulfhydryl Compounds | 2007 |
Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation.
Topics: Acid Phosphatase; Aluminum Oxide; Animals; Armoracia; Carbonic Anhydrases; Cattle; Enzyme Assays; Guanidine; Horseradish Peroxidase; Kinetics; Nanoparticles; Protein Conformation; Protein Denaturation; Protein Folding; Protein Renaturation; Solanum tuberosum | 2017 |