Autor: Stępiński, Janusz - Katalog OPAC zbiorów

Skocz do pozycji: 1.

Tytuł:: Badania metaloznawcze poznańskiego miecza św. Piotra z Muzeum Archidiecezjalnego w Poznaniu
A Metallurgical Study of the Poznań Sword of St. Peter from the Archdiocesan Museum in Poznań
Autorzy:: Nosek, Elżbieta M.
Stępiński, Janusz
Powiązania:: https://bibliotekanauki.pl/articles/1040231.pdf
Data publikacji:: 2011-01-01
Wydawca:: Uniwersytet im. Adama Mickiewicza w Poznaniu
Opis:: The authors present the results of a metallurgical study of the Poznań sword of St. Peter conducted in 2009. Analysis of the chemical composition of the metal of the blade helped to determine the technology used in its manufacture and consequently made it possible to specify the age and origin of the sword. The authors made an attempt to describe the sword of St. Peter and assign it to an adequate type of one blade weapons. In determining the presumed age of the sword a list of objects that resemble it visually (two 13th century cleavers) or are decorated with evidently related images (Greek vases) proved helpful.
Źródło:: Ecclesia. Studia z Dziejów Wielkopolski; 2011, 6; 77-103
1731-0679
Pojawia się w:: Ecclesia. Studia z Dziejów Wielkopolski
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 2.

Tytuł:: Badania metaloznawcze mieczy z cmentarzyska z okresu rzymskiego w Czelinie, woj. Zachodniopomorskie
Metallurgy study on swords from the Roman period burial ground in Czelin, West Pomeranian Voivodeship
Autorzy:: Biborski, Marcin
Kaczanowski, Piotr
Stępiński, Janusz
Powiązania:: https://bibliotekanauki.pl/articles/440571.pdf
Data publikacji:: 2015
Wydawca:: Muzeum Narodowe w Szczecinie
Tematy:: okres rzymski
miecze
typ Pompeje
typ Lachmirowice-Apa
typ Vimose-Illerup
Roman period
swords
Pompeii type
Lachmirowice-Apa type
Vimose-Illerup type
Opis:: Abstract: Results of the metallurgy study on three, two-edged swords from a cremation burial ground in Czelin, representing the Pompeii, Lachmirowice-Apa and Vimose-Illerup types indicate a variability in the material used as well as in technique of their production, and thus in the quality of the specimens. Two of them were made of a single piece of metal with low (specimen of the Lachmirowice-Apa type) or medium quality (specimen of the Pompeii type). A much higher level of craftsmanship is represented by the third sword of the Vimose-Illerup type, precisely forged from several pieces of diverse, high-quality material, representing the so-called pattern welding technique.
Źródło:: Materiały Zachodniopomorskie; 2014, 10; 133-157
0076-5236
Pojawia się w:: Materiały Zachodniopomorskie
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 3.

Tytuł:: Plant nucleoside 5-phosphoramidate hydrolase; simple purification from yellow lupin (Lupinus luteus) seeds and properties of homogeneous enzyme
Autorzy:: Guranowski, Andrzej
Wojdyła, Anna
Rydzik, Anna
Stepiński, Janusz
Jemielity, Jacek
Powiązania:: https://bibliotekanauki.pl/articles/1039966.pdf
Data publikacji:: 2011
Wydawca:: Polskie Towarzystwo Biochemiczne
Tematy:: yellow lupin
Lupinus luteus
adenosine 5'-phosphoramidate
purification to homogeneity
nucleoside 5'-phosphoramidase
Opis:: Adenosine 5'-phosphoramidate (NH2-pA) is an uncommon natural nucleotide of poorly understood biochemistry and function. We studied a plant enzyme potentially involved in the catabolism of NH2-pA. A fast and simple method comprising extraction of yellow lupin (Lupinus luteus) seed-meal with a low ionic strength buffer, ammonium sulfate and acetone fractionations, removal of contaminating proteins by heat denaturation, and affinity chromatography on AMP-agarose, yielded homogenous nucleoside 5'-phosphoramidase. Mass spectrometric analysis showed that the lupin hydrolase exhibits closest similarity to Arabidopsis thaliana Hint1 protein. The substrate specificity of the lupin enzyme, in particular its ability to split the P-S bond in adenosine 5'-phosphorothioate, is typical of known Hint1 proteins. Adenosine 5'-phosphofluoride and various derivatives of guanosine 5'-phosphoramidate were also substrates. Neither common divalent metal cations nor 10 mM EDTA or EGTA affected the hydrolysis of NH2-pA. The enzyme functions as a homodimer (2 × 15 800 Da). At the optimum pH of 7.0, the Km for NH2-pA was 0.5 µM and kcat 0.8 s-1 (per monomer active site). The properties of the lupin nucleoside 5'-phosphoramidase are compared with those of its counterparts from other organisms.
Źródło:: Acta Biochimica Polonica; 2011, 58, 1; 131-136
0001-527X
Pojawia się w:: Acta Biochimica Polonica
Dostawca treści:: Biblioteka Nauki

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