A Study of the Decay K°&lt;sub&gt;L&lt;/sub&gt; → πμν

Hill, D.

doi:10.2172/1447304

Cited by 4 publications

(4 citation statements)

References 2 publications

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“…The peptide SSSEE has been chosen as a reference because of its identity with a motif recurrent at several sites affected by CK-2 in casein and soybean antiprotease fractions [15], clathrin light chain-b [16] and the/~,subunit of CK-2 itself [12]. For both/~-casein [17] and synthetic peptides [18] this motif is mainly phosphorylated by CK-2 at its first serine in virtue of the penultimate glutamic acid fulfilling the minimum struc, tural requirement of an acidic residue at position +3.…”

Section: Resultsmentioning

confidence: 99%

Phosphotyrosine as a specificity determinant for casein kinase‐2, a growth related Ser/Thr‐specific protein kinase

et al. 1991

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The motif Ser‐Ser‐Ser‐Glu‐Glu is readily phosphorylated by casein kinase‐2 (CK‐2), a growth‐related protein kinase whose consensus sequence is Ser(Thr)‐Xaa‐Xaa‐Glu(Asp) [(1990) Biochim. Biophys. Acta. 1054, 267–283]. Here we show that phosphotyrosine can replace carboxylic acids as specificity determinant for CK‐2 phosphorylation, the phosphotyrosyl peptide Ser‐Ser‐Ser‐TyrP‐TyrP actually being a substrate more efficient than Ser‐Ser‐Ser‐Glu‐Glu itself both in terms of K m (0.69 vs 2.43 mM) and V???. Prior dephosphorylation of phosphotyrosine entirely prevents the subsequent phosphorylation of serine by CK‐2. While Ser‐Ser‐Ser‐TyrP‐TyrP is better than Ser‐Ser‐Ser‐SerP‐SerP, which in turn is better than Ser‐Ser‐Ser‐Glu‐Glu, Ser‐Ser‐Ser‐ThrP‐ThrP is a less efficient substrate than Ser‐Ser‐Ser‐Glu‐Glu. Thus the order of efficiency of phosphoamino acids as specificity determinants for CK‐2 appears to be TyrP>SerP>ThrP.

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Section: Resultsmentioning

confidence: 99%

Phosphotyrosine as a specificity determinant for casein kinase‐2, a growth related Ser/Thr‐specific protein kinase

et al. 1991

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“…The information on their structure is scarce. One of the best known glycosyltransferases is UDP-galactose : N-acetylglucosamine galactosyltransferase or A protein of the lactose synthetase complex (for review see [ 2 ] ) . This enzyme has been purified from various animal and human body fluids [3-81 but, with the exception of amino acid and carbohydrate content of the bovine milk enzyme [9], no additional information on the structure is available.…”

mentioning

confidence: 99%

The Charge Heterogeneity of Soluble Human Galactosyltransferases Isolated from Milk, Amniotic Fluid and Malignant Ascites

Gerber

Kozdrowski

Wyss

et al. 1979

European Journal of Biochemistry

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UDP-galactose: N-acetylglucosamine galactosyltransferase was isolated from pooled human milk, pooled amniotic fluid and from two different individual samples of malignant ascites. The purification procedure involving two successive affinity chromatography steps on N-acetylglucosamine -agarose and a-lactalbuniin -agarose yielded an enzyme preparation homogeneous by size. Under non-denaturing conditions the ascites and amniotic fluid enzymes had identical electrophoretic mobility, but they moved faster than the milk enzyme. Isoelectric analysis in the presence and absence of urea resolved the milk enzyme into at least 13 different forms, nine of which had the same isoelectric points after refocusing. All enzyme forms showed similar activity when free N-acetylglucosamine, ovalbumin, sialic-acid-free ovine submaxillary mucin and glucose, in the presence of a-lactalbumin, were used as acceptor substrates. Comparative isoelectric focusing of the three galactosyltransferases revealed identical patterns of the amniotic and ascites enzymes, but only partial overlap with the milk enzyme, which was less negatively charged. Neuraminidase treatment of ascites and milk galactosyltransferases produced very similar focusing patterns. The possible structural basis for this charge heterogeneity is briefly discussed.Biosynthesis of the heteropolysaccharide moieties of complex carbohydrates is catalyzed by glycosyltransferases (for review see [l]). The information on their structure is scarce. One of the best known glycosyltransferases is UDP-galactose : N-acetylglucosamine galactosyltransferase or A protein of the lactose synthetase complex (for review see [ 2 ] ) . This enzyme has been purified from various animal and human body fluids [3-81 but, with the exception of amino acid and carbohydrate content of the bovine milk enzyme [9], no additional information on the structure is available. Preliminary work indicated charge heterogeneity of galactosyltransferase as revealed by activity measurements of crude enzyme preparations which were subjected to isoelectric focusing [lo]. The present investigation was carried out in order to characterize the charge heterogeneity of pure galactosyltransferase. Since reports dealing with electrophoretic variants associated with cancer have recently been published [11--131, it seemed of interest to correlate the patterns obtained for the Abbreviations. Asialo-mucin, sialic-acid-free ovine submaxillary mucin; butyl-PBD, 2-(~-tert-butylphenyl)-5-(4-bisphenylyl)-1,3,4-oxadiazole.Enzynw. UDP-galactose :N-acetylglucosamine galactosyltransferase (EC 2.4.1.22). milk enzyme to the enzymes isolated from other sources, such as malignant ascites and amniotic fluid. The latter was chosen in order to investigate the possible occurrence of an onco-fetal variant in ascites (for review see [14]). The present work describes a higher electrophoretic mobility of galactosyltransferases from ascites and amniotic fluid under nondenaturing conditions when compared to the milk enzyme. This difference was due solely to ...

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“…The predominant white blood cells in milk consist of polymorphonuclear neutrophils and various types of lymphocytes, though others such as macrophages, are thought to be crucial for monitoring bacterial activity. E. coli is reasonably well processed and phagocytosed by the immune system (providing it responds quickly enough) (Hill et al, 1978;Shuster et al, 1996). On the other hand S. uberis is more resistant and can persist for some time despite these attentions (Hill 1981).…”

Section: Immunity and Mastitismentioning

confidence: 99%

Management: Animal health impacts of early lactation management - mastitis

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A Study of the Decay K°<sub>L</sub> → πμν

Cited by 4 publications

References 2 publications

Phosphotyrosine as a specificity determinant for casein kinase‐2, a growth related Ser/Thr‐specific protein kinase

Phosphotyrosine as a specificity determinant for casein kinase‐2, a growth related Ser/Thr‐specific protein kinase

The Charge Heterogeneity of Soluble Human Galactosyltransferases Isolated from Milk, Amniotic Fluid and Malignant Ascites

Management: Animal health impacts of early lactation management - mastitis

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