metalloprotein


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metalloprotein

 [mĕ-tal″o-pro´tēn]
a protein molecule bound to a metal ion, e.g., hemoglobin.

me·tal·lo·pro·tein

(mĕ-tal-ō-prō'tēn),
A protein with a tightly bound metal ion or ions; for example, hemoglobin.

me·tal·lo·pro·tein

(mĕ-tal'ō-prō'tēn)
A protein with a tightly bound metal ion or ions; e.g., hemoglobin.

metalloprotein

a PROTEIN containing a metal atom; examples are HAEMOGLOBIN, where the metal, iron, is a functional group, and ZINC FINGER, where the metal, zinc, is a structural feature. In addition, many ENZYMES require metal cations such as Ca++ @or Mg++ for activity.

me·tal·lo·pro·tein

(mĕ-tal'ō-prō'tēn)
A protein with a tightly bound metal ion or ions.
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References in periodicals archive ?
Metalloproteins (MT) were discovered by Margoshes and Valle (1957), who isolated them from the renal cortex of horses and identified them as proteins able to combine with cadmium (Cd).
Forge Therapeutics CEO, Zachary Zimmerman, said "We are pleased to obtain exclusive worldwide rights to this intellectual property, which adds to our expanding and dominant patent portfolio protecting the development and commercialization of metalloprotein inhibitors.
Adams, "A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involved in hydrogen production from pyruvate," Biochemistry, vol.
(22) Chrysoeriol has been shown to be an effective inhibitor of the matrix metalloprotein that damages collagen and elastin and cause premature skin aging.
Casein also aids the absorption of vitamins and minerals and is vital to the production of haemoglobin, the metalloprotein in red blood cells that transports oxygen around the body.
Using a viral vector, Ahrens incorporated the gene that produces the naturally occurring metalloprotein ferritin into living cells.
All ESAs aim to improve oxygen transport by the metalloprotein hemoglobin.
Specialists in drug design and discovery of zinc metalloprotein inhibitors report on research findings that have emerged over the past few years at a level accessible to academic or industrial researchers and to graduate students.
Serum alkaline phosphatase is a member of a family of zinc metalloprotein enzymes that function to split off a terminal phosphate group from an organic phosphate ester.
It is an iron-containing, tetrameric metalloprotein that consists of two pairs of unlike globin chains (i.e., two [alpha]-type and two [beta]-type globin chains).
An increased absorption of zinc from zinc-methionine complex may lead to a larger zinc pool, thereby increasing zinc metalloprotein activities, plasma levels of zinc and immune cell functions that require zinc (Kidd et al., 1996).
After entering into the lysosome, it undergoes stimulates the synthesis of more metalloprotein in the tubule cells and becomes linked to it (Cherian & Shaikh; Nordberg and Foulkes) but the intercellular metal, not bound to metallothionein, increases when its concentration exceeds the capacity of the proximal tubular cells to synthesize metallothionein (Shaikh, 1982).

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