Alpha-amylase E.C.3.2.1.1. (1,4 glucan, 4 glucanohydrolase) can be obtained from salivary glands, pancreas and microorganisms such as Pseudomonas and Asperigllus, as well as muscles and ovarian tubes.1.2 Alpha-amylase from Bacillus Subtilis #1024(A TCC 465)* was purified with a highest degree of purity in our laboratory (31.59 U/mg). The extracellular alpha-amylase was subjected to differe...

the binding of sodium n-dodecyl sulphate (sds) to aspergillus niger catalase in various ionic strengths at ph 6.4 and a temperature of 27? and 37?c has been studied over a range of sds concentrations using equilibrium dialysis and fluorescence spectroscopy techniques. the binding data were used and interpreted in terms of theoretical models (scatchard equation and wyman binding potential). the ...

1. N-Acetylgalactosamine 6-sulphate sulphatase was purified about 20000-fold from the soluble extract of human placenta with N-acetylgalactosamine 6-sulphate-glucuronic acid-N-acetyl[1-(3)H]galactosaminitol 6-sulphate as substrate in the activity assay. The enzyme appears to be a glycoprotein with a mol.wt. of about 100000 as determined by gel filtration. On gel electrophoresis in the presence ...

1. The enzymic activity of glucose oxidase was determined as a function of pH and sodium n-dodecyl sulphate (SDS) concentration. 2. Glucose oxidase is not deactivated by SDS at pH 6 even after prolonged incubation, but is deactivated at pH 4.3 and 3.65. 3. Sedimentation-rate analysis showed that glucose oxidase dissociates into its two subunits at pH 5 and below, and sedimentation-equilibrium e...

The technique of three-phase partitioning (TPP) was used to purify the green fluorescent protein (GFP) in a single step. TPP uses a combination of ammonium sulphate and tert-butanol to precipitate proteins from their crude extracts. In the first round of TPP with 20% ammonium sulphate saturation at the ratio of crude to tert-butanol 1:1 (v/v), most of the GFP remains in the lower aqueous phase....

The binding of bovine testicular hyaluronidase to AH-Sepharose (1,6-diaminohexane--Sepharose) gels substituted with (1) dermatan sulphate, (2) desulphated dermatan sulphate, (3) heparin and (4) de-N/O-sulphated, re-N-acetylated heparin was investigated. Hyaluronidase was found to bind to (1) and (3), but not (2) and (4). On the basis of these observations a preparative scheme for the purificati...