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1.
Biochem J ; 242(2): 353-60, 1987 Mar 01.
Artigo em Inglês | MEDLINE | ID: mdl-3593255

RESUMO

The crystal structure of baboon alpha-lactalbumin has been determined at 6 A and at 4.5 A (0.6 nm and 0.45 nm) resolution by the method of isomorphous replacement. The principal derivative was prepared by reducing a disulphide bridge in the crystals and inserting a mercury atom. Detailed comparison of the electron-density maps with corresponding maps of hen egg-white lysozyme shows that they are closely similar, with correlation coefficients of 0.57 and 0.44 at 6 A and 4.5 A resolution respectively. This result, in accordance with earlier predictions based upon comparisons of amino-acid sequences, provides further evidence that class C lysozymes and alpha-lactalbumins are homologous proteins and it is in keeping with the hypothesis that the alpha-lactalbumins evolved from a lysozyme precursor.


Assuntos
Lactalbumina , Sequência de Aminoácidos , Animais , Modelos Moleculares , Muramidase , Papio , Conformação Proteica , Difração de Raios X
2.
Biochim Biophys Acta ; 625(1): 64-71, 1980 Sep 23.
Artigo em Inglês | MEDLINE | ID: mdl-7417502

RESUMO

Lysozyme extracted from the egg-white of tortoise, the first example of a reptilian lysozyme to have been purified, has been crystallized and its tertiary structure determined at low resolution by X-ray analysis. This structure is shown to be closely homologous to that of hen egg-white lysozyme. The crystals of tortoise egg-white lysozyme contain a large proportion of liquid and the X-ray map shows that this forms large channels through the crystals into which the active sites of the enzyme molecules open. This indicates that tortois lysozyme crystals may be suitable for low-temperature studies of true enzyme substrate complexes.


Assuntos
Muramidase/isolamento & purificação , Ovalbumina/análise , Óvulo/enzimologia , Animais , Feminino , Tartarugas , Difração de Raios X
4.
Biochem J ; 181(2): 497-9, 1979 Aug 01.
Artigo em Inglês | MEDLINE | ID: mdl-496896

RESUMO

The Fv fragment of mouse myeloma protein M313 was crystallized from poly(ethylene glycol) solution in the form of monoclinic crystals, space group C2 and unit cell dimensions a = 5.96 nm (59.6 A), b = 5.66 nm (56.6 A), c = 13.79 nm (13.9 A) and beta = 99.7 degrees. Some unusual effects of poly(ethylene glycol)on protein crystals were noted and are discussed.


Assuntos
Fragmentos de Imunoglobulinas , Proteínas do Mieloma , Animais , Fenômenos Químicos , Química , Cristalização , Camundongos , Polietilenoglicóis
11.
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