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Source: The Open Library

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1The peanut plant and light

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“The peanut plant and light” Metadata:

  • Title: The peanut plant and light
  • Author:
  • Language: English
  • Publisher: Nova Science Publishers
  • Publish Date:
  • Publish Location: Hauppauge, N.Y

“The peanut plant and light” Subjects and Themes:

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  • First Year Published: 2010
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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2The peanut plant and light

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“The peanut plant and light” Metadata:

  • Title: The peanut plant and light
  • Author:
  • Language: English
  • Number of Pages: Median: 62
  • Publisher: Nova Science Publishers
  • Publish Date:
  • Publish Location: New York

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Access and General Info:

  • First Year Published: 2010
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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3Studies on the metabolism of 1,4-¹⁴C-spermidine and 1,4-¹⁴C-spermine in the rat

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“Studies on the metabolism of 1,4-¹⁴C-spermidine and 1,4-¹⁴C-spermine in the rat” Metadata:

  • Title: ➤  Studies on the metabolism of 1,4-¹⁴C-spermidine and 1,4-¹⁴C-spermine in the rat
  • Author:
  • Language: English
  • Number of Pages: Median: 66
  • Publish Date:
  • Publish Location: Helsinki

“Studies on the metabolism of 1,4-¹⁴C-spermidine and 1,4-¹⁴C-spermine in the rat” Subjects and Themes:

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  • First Year Published: 1967
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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4Synthesis and evaluation of spermidine siderophores for iron chelation therapy and the role of cyclohexaamylose in catalytic hydrolysis

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“Synthesis and evaluation of spermidine siderophores for iron chelation therapy and the role of cyclohexaamylose in catalytic hydrolysis” Metadata:

  • Title: ➤  Synthesis and evaluation of spermidine siderophores for iron chelation therapy and the role of cyclohexaamylose in catalytic hydrolysis
  • Author:
  • Language: English
  • Number of Pages: Median: 152
  • Publisher: Gainesville, FL
  • Publish Date:

“Synthesis and evaluation of spermidine siderophores for iron chelation therapy and the role of cyclohexaamylose in catalytic hydrolysis” Subjects and Themes:

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Access and General Info:

  • First Year Published: 1981
  • Is Full Text Available: Yes
  • Is The Book Public: Yes
  • Access Status: Public

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    Wiki

    Source: Wikipedia

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    Spermidine

    Spermidine is a polyamine compound (C 7H 19N 3) found in ribosomes and living tissues and having various metabolic functions within organisms. Spermidine

    Polyamine

    are found in all forms of life. The principal examples are the triamine spermidine and the tetraamine spermine. They are structurally and biosynthetically

    Spermidine synthase

    Spermidine synthase is an enzyme (EC 2.5.1.16) that catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the

    Putrescine

    described. Spermidine synthase uses putrescine and S-adenosylmethioninamine (decarboxylated S-adenosyl methionine) to produce spermidine. Spermidine in turn

    SAT1 (gene)

    Diamine acetyltransferase 1 (also termed spermidine/spermine N(1)-acetyltransferase 1, SSAT, and SAT1) is an enzyme that in humans is encoded by the SAT1

    Spermine oxidase

    AtPAO1, AtPAO4, SMO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (spermidine-forming). This enzyme catalyses the following chemical

    Trypanothione

    form of glutathione containing two molecules of glutathione joined by a spermidine (polyamine) linker. It is found in parasitic protozoa such as leishmania

    Spermidine dehydrogenase

    In enzymology, a spermidine dehydrogenase (EC 1.5.99.6) is an enzyme that catalyzes the chemical reaction spermidine + acceptor + H2O ⇌ {\displaystyle

    Glutathionylspermidine synthase

    1.8) is an enzyme that catalyzes the chemical reaction glutathione + spermidine + ATP ⇌ {\displaystyle \rightleftharpoons } glutathionylspermidine + ADP

    S-Adenosylmethioninamine

    substrate that is required for the biosynthesis of polyamines including spermidine, spermine, and thermospermine. It is produced by decarboxylation of S-adenosyl