Effect of Sodium Dodecyl Sulphate on the Hydrolysis of Procaine

1990 ◽  
Vol 27 (2) ◽  
pp. 108-112
Author(s):  
N. Razvi ◽  
A. E. Beg
1978 ◽  
Vol 175 (3) ◽  
pp. 1023-1032 ◽  
Author(s):  
P Knight ◽  
G Offer

Covalent cross-links can be inserted between the subunits of F-actin by using p-NN′-phenylenebismaleimide. Cross-linking reaches its maximum value when one molecule of reagent has reacted with each actin subunit. p-NN′-Phenylenebismaleimide reacts initially with a cysteine residue on one subunit, the slower cross-linking reaction involving a lysine residue on a neighbouring subunit. Hydrolysis of the actin-bound reagent limits the extent of cross-linking. Quantitative analysis of the amounts of cross-linked oligomers seen on polyacrylamide gels containing sodium dodecyl sulphate suggests that neither the binding of the reagent to actin nor the formation of cross-links introduces strain into the structure. The cross-links do not join together different F-actin filaments, and evidence is presented that suggests that the cross-links join subunits of the same long-pitched helix.


1977 ◽  
Vol 161 (1) ◽  
pp. 123-130 ◽  
Author(s):  
R J S Julian

A steroid-sensitive aldehyde dehydrogenase (EC 1.2.1.3) was purified from rabbit liver and is homogeneous by the criterion of electrophoresis in polyacrylamide gels with or without sodium dodecyl sulphate. The enzyme is tetrameric, of subunit mo.wt. 48 300, and contains no tightly bound zinc. The fluorescence of the protein is decreased in the presence of progesterone, which is inhibitory to the reactions catalysed by the enzyme. When NADH is bound to the enzyme, the fluorescence of the coenzyme is augmented to an extent independent of the presence of steroids or acetaldehyde. The purified enzyme catalyses the oxidation of acetaldehyde and glucuronolactone, and the hydrolysis of 4-nitrophenyl acetate. Each of these reactions is inhibited by progesterone in such a manner as to suggest the formation of a catalytically active enzyme-hormone complex. Diethylstilboestrol inhibits the hydrolysis of esters by this enzyme, but stimulates the oxidation of aldehydes, except at low aldehyde concentrations; the ligand is then inhibitory. NADH inhibits the hydrolysis of 4-nitrophenyl acetate by the enzyme in a partially competitive fashion.


1986 ◽  
Vol 53 (2) ◽  
pp. 249-258 ◽  
Author(s):  
Lesley C. Chaplin ◽  
Richard L. J. Lyster

SUMMARYThe irreversible heat denaturation of α-lactalbumin (α-la) in 0·1 M-phosphate, pH 7·0, at 100 °C was studied using polyacrylamide-gel electrophoresis (PAGE). PAGE revealed two groups of bands, one moving faster than native α-la and one slower, in addition to some denatured protein which remained at the origin and some residual native α-la. The faster group had unchanged molecular weight, but an increase in charge, partly due to hydrolysis of glutamine and asparagine residues. The slower group was shown by two-dimensional sodium dodecyl sulphate-PAGE to be oligomers of denatured α-la; formation of the smaller oligomers preceded the larger ones. The oligomers reverted to monomers in the presence of dithiothreitol, showing that they were disulphide-linked aggregates of denatured α-la. Immuno-blots of the gels showed that both fast and slow groups of bands had irreversibly lost most of the antigenicity of the native protein.


1975 ◽  
Vol 149 (2) ◽  
pp. 397-401 ◽  
Author(s):  
R Virden ◽  
A F Bristow ◽  
R H Pain

1. The penicillinase-catalysed hydrolysis of quinacillin was quenched by addition of 5 m-guanidinium chloride or 1% (w/v) sodium dodecyl sulphate, and the quenched reaction mixture was dialysed exhaustively against solutions of the denaturant. 2. Irreversibly bound quinacillin was shown by titration with HgCl2 to be covalently attached to the protein by the β-lactam carboxyl group. 3. The derivative was found to be stable over the pH range 3.5-8.5. 4. Chymotryptic hydrolysis of the product and subsequent fractionation showed that quinacillin was bound to one or possibly two peptides.


Author(s):  
Mira Ristić ◽  
Jasenka Štajdohar ◽  
Ivana Opačak ◽  
Svetozar Musić

Precipitations by the forced hydrolysis of 0.2 M FeCl3 aqueous solutions between 2 and 72 hours in the presence of 1% sodium dodecyl sulphate (SDS) were investigated. In the absence of SDS a direct phase transformation ß-FeOOH → α-Fe2O3 via dissolution/recrystallization occured in the precipitation system. In the presence of SDS, α-FeOOH as an intermediate phase precipitated and, with a prolonged time of forced hydrolysis, also transformed to α-Fe2O3 via the dissolution/recrystallization mechanism. On the basis of Mössbauer spectra it was concluded that in the presence of SDS, α-Fe2O3 phase possessed a lower degree of crystallinity. In this precipitation process the competition between the stability of Fe(III)-dodecyl sulphate, on one side, and the formation of iron oxide phases, on the other, also played an important role. FE SEM revealed that the big α-Fe2O3 particles possessed the substructure. The elongation of primary α-Fe2O3 particles produced in the presence of SDS was noticed. This effect can be assigned to the preferential adsorption of dodecyl sulphate groups on nuclei and crystallites of FeOOH and α-Fe2O3 phase during the forced hydrolysis of FeCl3 solutions.


2018 ◽  
Vol 91 (3) ◽  
Author(s):  
Mira Ristić ◽  
Jasenka Štajdohar ◽  
Ivana Mitar ◽  
Svetozar Musić

Development ◽  
1986 ◽  
Vol 92 (1) ◽  
pp. 183-191
Author(s):  
C. R. Brown ◽  
W. K. T. Cheng

Our objective was to identify any changes that occur in the composition of the porcine zona pellucida during development of the 2- to 4-cell embryo from the oocyte. Oocytes, unfertilized eggs and single and 2- to 4-cell embryos have been recovered surgically and their zonae pellucidae 125I-labelled and analysed individually by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The zonae from ovulated eggs possessed two major glycoproteins Mr 250000 and 90000 which were absent from follicular oocytes but present in the fluid from the oestrus, but not luteal, oviduct. The glycoproteins remained on the zona pellucida of 2- to 4-cell embryos whose analysis showed the presence of additional polypeptides of Mr 150000, 57000, 50000 and 25000. It is concluded (i) that shortly after ovulation, and in spite of the presence around the egg of cumulus oophorus and corona radiata cells, significant amounts of oviducal glycoproteins are able to bind firmly to the zona pellucida, and (ii) that after contact with spermatozoa there is evidence of a limited hydrolysis of the structure by the sperm protease acrosin.


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