[52] Glyceraldehyde-3-phosphate dehydrogenase from human tissues

Heinz, Fritz; Freimüller, B

doi:10.1016/s0076-6879(82)89054-x

Cited by 45 publications

(24 citation statements)

References 2 publications

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“…This suggests possible differences in the mechanism of the catalytic reaction. Therefore, some catalytic features of the GAPDH of the two marine species reported here differ from those previously described for GAPDH from other sources [36][37][38]43], reflecting protein differences between species.…”

Section: Discussioncontrasting

confidence: 85%

“…However, the sardine enzyme subunit exhibited an estimated molecular mass of 37 kDa that is somewhat higher than the one reported for bacterial and molluscan species (ca. 35 kDa), but is identical to those reported for the amphibian (pleurodeles) and mammalian ( jerboa or human) species GAPDHs [33,36,38]. Moreover, the isoelectric focusing technique revealed very different values of pI for the single protein band present in the enzyme preparations purified from the two species, namely 7.9 and 6.6 for sardine and octopus GAPDH, respectively.…”

Section: Discussionsupporting

confidence: 78%

“…The kinetic parameters of octopus and sardina GAPDH (K m values for D-G3P and NAD þ being, respectively, in the ranges of 70 mM-300 mM and 70 mM-90 mM) ( Table 2) are comparable to those found for cytosolic GAPDHs purified from other eukaryotes, protists (Tetrahymena pyriformis [43]), lower metazoa like the mollusk Loligo vulgaris [47], or mammalians like Jaculus orientalis or Homo sapiens [36,38]. However, on the whole the kinetic parameters analyses show that the octopus enzyme is catalytically less efficient than GAPDH of sardine.…”

Section: Discussionsupporting

confidence: 54%

“…A single GAPDH isoform has been previously found in other animal tissues and microorganisms, both prokaryotes and eukaryotes [4,33,44,45]. However, it does not seem to be a general rule, as the presence of several GAPDH isoforms have also been reported in phylogenetically different organisms [37,38,45,46].…”

Section: Discussionmentioning

confidence: 99%

See 3 more Smart Citations

Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from <italic>Sardina pilchardus</italic> and <italic>Octopus vulgaris</italic>

Baibai¹,

Oukhattar²,

Mountassif³

et al. 2010

ABBS

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Section: Discussioncontrasting

confidence: 85%

Section: Discussionsupporting

confidence: 78%

Section: Discussionsupporting

confidence: 54%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from <italic>Sardina pilchardus</italic> and <italic>Octopus vulgaris</italic>

Baibai¹,

Oukhattar²,

Mountassif³

et al. 2010

ABBS

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“…Protein sequencing was carried out by the University of Michigan Carbohydrate Facility using acid hydrolysis followed by high-performance liquid chromatography. GAPDH enzyme assays were performed according to Heinz and Freimuller [14].…”

Section: Miscellaneous Proceduresmentioning

confidence: 99%

Identification of glyceraldehyde-3-phosphate dehydrogenase as a Ca2+-dependent fusogen in human neutrophil cytosol

Hessler

Blackwood

Brock

et al. 1998

Journal of Leukocyte Biology

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The membrane fusion events observed during neutrophil degranulation are important aspects of the immunoregulatory system. In an attempt to understand the regulation of granuleplasma membrane fusion, we have begun characterizing human neutrophil cytosol for fusion activity, finding that 50% of the fusogenic activity could be attributed to members of the annexin family of proteins. The major non-annexin fusion activity (25% of the total cytosolic activity) was enriched by ion exchange chromatography after depletion of annexins by Ca 2؉ -dependent phospholipid affinity chromatography. The fusion activity co-purified with a 10,14-kDa dimer identified as leukocyte L1 (which was non-fusogenic), along with an approximately 36-kDa protein. This protein was identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by amino-terminal sequencing, and the fusion activity was verified using commercially available GAPDH. GAPDH may play an important role in degranulation because it is as potent as annexin I on a mass basis and may constitute up to 25% of the total cytosolic fusion activity of the neutrophil. J.

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Purification and Characterization

Tsai

2006

Biomacromolecules

208

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Idiomarina loihiensis was isolated from the salt works in Sfax (Tunisia), until now, the characterization of the GAPDH phosphorylante was never studied. Here, we report the isolation and the biochemical characterization of glyceralehyde-3-phosphate dehydrogenase (GAPDH) from I. loihiensis saline's bacteria on the basis of the apparent native and subunit molecular weights, physico-chemical and kinetic characterizations. The purification method consisted of two steps, ammonium sulfate fractionation followed by one chromatographic step, namely dye-affinity on Blue Sepharose CL-6B. Polyclonal antibodies against the purified enzyme were used to recognize the I. loihiensis GAPDH by Western blotting. The optimum pH of the purified enzyme was 8.5. Studies on the effect of temperatures revealed an enzyme increasing activity of about 45˚C. The molecular weight of the purified enzyme was 36 kDa determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Non-denaturing polyacrylamide gels yield a molecular weight of 147 kDa. The Michaelis constants for NAD + and D-glyceraldehyde-3-phosphate estimated was 19 μM and 3.1 μM, respectively. The maximal velocity of the purified enzyme was estimated to be 2.06 U/mg, approximately 6-fold increase in specific activity and a final yield of approximately 32.5%. The physicochemical properties of this GAPDH, being characterized, could be used in further studies.

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[52] Glyceraldehyde-3-phosphate dehydrogenase from human tissues

Cited by 45 publications

References 2 publications

Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from <italic>Sardina pilchardus</italic> and <italic>Octopus vulgaris</italic>

Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from <italic>Sardina pilchardus</italic> and <italic>Octopus vulgaris</italic>

Identification of glyceraldehyde-3-phosphate dehydrogenase as a Ca2+-dependent fusogen in human neutrophil cytosol

Purification and Characterization

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[52] Glyceraldehyde-3-phosphate dehydrogenase from human tissues

Cited by 45 publications

References 2 publications

Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from &lt;italic&gt;Sardina pilchardus&lt;/italic&gt; and &lt;italic&gt;Octopus vulgaris&lt;/italic&gt;

Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from &lt;italic&gt;Sardina pilchardus&lt;/italic&gt; and &lt;italic&gt;Octopus vulgaris&lt;/italic&gt;

Identification of glyceraldehyde-3-phosphate dehydrogenase as a Ca2+-dependent fusogen in human neutrophil cytosol

Purification and Characterization

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Product

Resources

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Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from <italic>Sardina pilchardus</italic> and <italic>Octopus vulgaris</italic>

Comparative molecular analysis of evolutionarily distant glyceraldehyde-3-phosphate dehydrogenase from <italic>Sardina pilchardus</italic> and <italic>Octopus vulgaris</italic>