<?xml version="1.0"?>
<rss version="2.0">
   <channel>
      <title>Bookmarks by Creative Enzymes Lisa Clara</title>
      <link>https://padlet.com/contact255/Bookmarks</link>
      <description></description>
      <language>en-us</language>
      <pubDate>2017-08-17 09:48:19 UTC</pubDate>
      <lastBuildDate>2023-01-21 21:53:03 UTC</lastBuildDate>
      <webMaster>hello@padlet.com</webMaster>
      <image>
         <url></url>
      </image>
      <item>
         <title>native thio-nadp</title>
         <author>contact255</author>
         <link>https://padlet.com/contact255/Bookmarks/wish/185798070</link>
         <description><![CDATA[<div>Thio-Nicotinamide-Adenine Dinucleotide Phosphate, Oxidized (Thio-NADP); Thio-Nicotinamide-Adenine Dinucleotide Phosphate; Thio-NADP</div>]]></description>
         <enclosure url="http://www.creative-enzymes.com/similar/ThioNADP_779.html" />
         <pubDate>2017-09-08 09:11:18 UTC</pubDate>
         <guid>https://padlet.com/contact255/Bookmarks/wish/185798070</guid>
      </item>
      <item>
         <title>Papain meat tenderizer</title>
         <author>contact255</author>
         <link>https://padlet.com/contact255/Bookmarks/wish/185798257</link>
         <description><![CDATA[<div>Papain papaya latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.</div>]]></description>
         <enclosure url="http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html" />
         <pubDate>2017-09-08 09:12:11 UTC</pubDate>
         <guid>https://padlet.com/contact255/Bookmarks/wish/185798257</guid>
      </item>
      <item>
         <title>Carboxypeptidase g</title>
         <author>contact255</author>
         <link>https://padlet.com/contact255/Bookmarks/wish/201117204</link>
         <description><![CDATA[<div>Carboxypeptidase G is a lysosomal, thiol-dependent protease, which progressively cleaves γ-glutamyl pteroyl poly-γ-glutamate yielding pteroyl-α-glutamate (folic acid) and free glutamate. It is considered highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid of the leaving group.1 Molecular mass of this homodimer is approximately 90 kDa. The enzyme is activated by Zn2+ ions.</div>]]></description>
         <enclosure url="https://www.creative-enzymes.com/similar/Carboxypeptidase-G_97.html" />
         <pubDate>2017-10-27 08:35:01 UTC</pubDate>
         <guid>https://padlet.com/contact255/Bookmarks/wish/201117204</guid>
      </item>
      <item>
         <title>Hyaluronate lyase</title>
         <author>contact255</author>
         <link>https://padlet.com/contact255/Bookmarks/wish/201117965</link>
         <description><![CDATA[<div>Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. It is important for the diffusion of toxins and proteins produced by S. pyogenes.</div>]]></description>
         <enclosure url="https://www.creative-enzymes.com/similar/Hyaluronate-Lyase_365.html" />
         <pubDate>2017-10-27 08:38:55 UTC</pubDate>
         <guid>https://padlet.com/contact255/Bookmarks/wish/201117965</guid>
      </item>
      <item>
         <title>Enzyme trypsin</title>
         <author>contact255</author>
         <link>https://padlet.com/contact255/Bookmarks/wish/201118176</link>
         <description><![CDATA[<div><br>Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. </div>]]></description>
         <enclosure url="https://www.creative-enzymes.com/product/native-bovine-trypsin_944.html" />
         <pubDate>2017-10-27 08:39:59 UTC</pubDate>
         <guid>https://padlet.com/contact255/Bookmarks/wish/201118176</guid>
      </item>
      <item>
         <title>enolase</title>
         <author>contact255</author>
         <link>https://padlet.com/contact255/Bookmarks/wish/215689811</link>
         <description><![CDATA[<div>Description:<br><br>Enolase is a metalloenzyme that catalyzes the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Enolase is essential for both glycolysis and gluconeogenesis. Enolase from baker’s yeast is a homodimer containing two bound Mg2+ ions. The molecular weight is 93.069 kDa.The peptide consists of 436 amino acids and contains a single cysteine residue. Two of the active site components include His191 and Arg414. The phosphorylated tyrosine residue present in yeast enolase forms a substrate for phosphorylation by tyrosine protein kinase. Apart from Mg2+, the enzyme can be activated by Zn2+, Mn2+, and Cd2+.<br>More: </div>]]></description>
         <enclosure url="" />
         <pubDate>2017-12-13 07:49:42 UTC</pubDate>
         <guid>https://padlet.com/contact255/Bookmarks/wish/215689811</guid>
      </item>
      <item>
         <title>phospholipase a2</title>
         <author>contact255</author>
         <link>https://padlet.com/contact255/Bookmarks/wish/221589926</link>
         <description><![CDATA[<div><br>Hydrolysis by Phospholipase A2 (food grade) converts the phospholipid into a stable lysopholipid with strongly improved emulsifiying thermo stable properties.<br><a href="https://www.creative-enzymes.com/similar/PLA2_575.html">https://www.creative-enzymes.com/similar/PLA2_575.html</a></div>]]></description>
         <enclosure url="https://padletuploads.blob.core.windows.net/prod/214871290/b916db6242af23ca74f85ed2c46e4f17/phospholipase_a2.jpg" />
         <pubDate>2018-01-16 06:41:59 UTC</pubDate>
         <guid>https://padlet.com/contact255/Bookmarks/wish/221589926</guid>
      </item>
   </channel>
</rss>
