Enzyme & protein最新文献_第9页

Concentration of white blood cell UDPgalactose and UDPglucose determined by high performance liquid chromatography. 高效液相色谱法测定白细胞udp半乳糖和udp葡萄糖浓度。

Enzyme & protein Pub Date : 1993-01-01 DOI: 10.1159/000468666

M J Palmieri, R A Reynolds, J B Gibson, G T Berry, S Segal

{"title":"Concentration of white blood cell UDPgalactose and UDPglucose determined by high performance liquid chromatography.","authors":"M J Palmieri, R A Reynolds, J B Gibson, G T Berry, S Segal","doi":"10.1159/000468666","DOIUrl":"https://doi.org/10.1159/000468666","url":null,"abstract":"We have applied a HPLC method to separate and quantitate UDPgalactose (UDPGal) and UDPglucose (UDPGlu) in human white blood cells (WBCs). Trichloroacetic acid-treated, protein-free filtrates were chromatographed on an anion-exchange column (Dionex CarboPac PA-1) using a gradient of 20-40% potassium phosphate buffer (pH 4.5). Recoveries of UDPGal and UDPGlu ranged from 93 to 106%, and the method was linear over a wide range of WBC protein concentrations. Volumes of blood as low as 2.5 ml (2.2 mg WBC protein) could be used to achieve quantitative recovery of the sugar nucleotides. The mean values and standard deviations of UDPGal and UDPGlu in 33 normal individuals ranging in age from 1 day to 65 years were 12.4 +/- 4.2 and 31.5 +/- 9.3 mumol/100 g protein, respectively. No statistical differences in UDPGal and UDPGlu values were observed between children and adults. No correlation was established between the concentrations of UDPGal and UDPGlu and either total WBC count or the number of lymphocytes obtained from Coulter counter analysis. There was no relationship between the concentrations of UDPGal and UDPGlu in WBCs and RBCs which were prepared from the same blood specimen.","PeriodicalId":11854,"journal":{"name":"Enzyme & protein","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1993-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000468666","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19080625","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Postnatal expression of hypoxanthine guanine phosphoribosyltransferase in the mouse brain. 产后小鼠脑内次黄嘌呤鸟嘌呤磷酸核糖转移酶的表达。

Enzyme & protein Pub Date : 1993-01-01 DOI: 10.1159/000468659

K Ikeda, T Iida, S Nakagawa

{"title":"Postnatal expression of hypoxanthine guanine phosphoribosyltransferase in the mouse brain.","authors":"K Ikeda, T Iida, S Nakagawa","doi":"10.1159/000468659","DOIUrl":"https://doi.org/10.1159/000468659","url":null,"abstract":"The distributional and activity changes of hypoxanthine guanine phosphoribosyltransferase (HGPRT) were investigated in the developing mouse brain. The HGPRT activity level was low at birth, increased rapidly during the first 7 days of life, and underwent a gradual increase thereafter to the mature level. Polyclonal antibody against HGPRT purified from mouse brain was prepared for immunohistochemical demonstration of the enzyme during brain development. In the cerebellum, part of the Purkinje cells was consistently immunostained throughout growth, and the presence of HGPRT was observed in the dendrites of mature Purkinje cells. The most dominant change in HGPRT localization was observed in the hippocampus. Little HGPRT was detectable in the newborn mouse hippocampus. At postnatal day 7, cytoplasmic HGPRT appeared sporadically in the granular cells independently of the region of the hippocampus. The number of positive immunoreactive cells increased with growth, and the dendrites of granular cells were also immunostained on postnatal day 28. Further immunostaining was noted in the granule cells of the dentate gyrus on postnatal day 35. The above results suggest that HGPRT may play an important role in the developing hippocampus. Further investigations of the HGPRT in the human hippocampus may help to clarify the mechanism underlying the neurological disorders encountered in the Lesch-Nyhan syndrome.","PeriodicalId":11854,"journal":{"name":"Enzyme & protein","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1993-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000468659","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19185684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Two-dimensional polyacrylamide gel electrophoresis isolation and microsequencing of Pseudomonas aeruginosa proteins. 铜绿假单胞菌蛋白的双向聚丙烯酰胺凝胶电泳分离及微测序。

Enzyme & protein Pub Date : 1993-01-01 DOI: 10.1159/000468649

M Michéa-Hamzehpour, J C Sanchez, S F Epp, N Paquet, G J Hughes, D Hochstrasser, J C Pechère

引用次数: 12

Analysis of errors in the calculation of irreversible enzyme inhibition kinetic constants. 不可逆酶抑制动力学常数计算误差分析。

Enzyme & protein Pub Date : 1993-01-01 DOI: 10.1159/000468667

P J Gray, D R Skinner, K K Benke

引用次数: 3

Structural features of 26S and 20S proteasomes. 26S和20S蛋白酶体的结构特征。

Enzyme & protein Pub Date : 1993-01-01 DOI: 10.1159/000468684

A Lupas, A J Koster, W Baumeister