Pteris deflexa 15 claims

species · family Pteridaceae · green plant · NCBI Taxonomy ↗

2 spellings

Pteris deflexaAndrés González · CC BY-SA 4.0 · Wikimedia Commons ↗

15 claims

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Observationobservedoriginal resultmeasured

Claim · model-written summary

Acid invertase was evident mainly in the phloem of Pteris deflexa vascular tissue.

Taxon: Pteris deflexaPteris deflexat0
Organ / stage: vascular tissue, mainly in phloeme0
Gene: Acid invertasee0
Outcome: Acid invertasee0

Verbatim

e0
“Acid invertase, localized by immuno-histochemical and histochemical techniques on fresh tissues, was evident in vascular tissue, mainly in phloem.”
✓ located verbatim in the source · abstract, characters 389–535

t0
“Pteris deflexa Link”
✓ located verbatim in the source · title, characters 50–69

Title

Acid invertase localization in leaves of the fern Pteris deflexa Link

JE Sayago; RM Ordóñez; MI Isla European Journal of Histochemistry 2009. doi:10.4081/1225

Other claims from this paper (2)

Observationobservedoriginal resultmeasured

Claim · model-written summary

Acid invertase was also detected in cells of the petiole, rachis, rachis branches, and leaf blade veins.

Taxon: Pteris deflexaPteris deflexat0
Organ / stage: parenchymatic, sclerenchymatic and epidermic cells of petiole, rachis and rachis branches as well as in veins of leaf bladese0
Outcome: detectede0

Verbatim

e0
“It was also detected in parenchymatic, sclerenchymatic and epidermic cells of petiole, rachis and rachis branches as well as in veins of leaf blades.”
✓ located verbatim in the source · abstract, characters 536–685

t0
“Pteris deflexa Link”
✓ located verbatim in the source · title, characters 50–69

Title

Acid invertase localization in leaves of the fern Pteris deflexa Link

JE Sayago; RM Ordóñez; MI Isla European Journal of Histochemistry 2009. doi:10.4081/1225

Other claims from this paper (2)

Observationauthor interpretationoriginal resultmeasured

Claim · model-written summary

Acid invertase localization in P. deflexa was similar to that of higher plants.

Taxon: P. deflexaPteris deflexae0
Outcome: acid invertase localizatione0
Direction: the samee0
Comparator: higher plantse0

Verbatim

e0
“Our results demonstrate that P. deflexa acid invertase localization is the same to that of higher plants.”
✓ located verbatim in the source · abstract, characters 686–791

Title

Acid invertase localization in leaves of the fern Pteris deflexa Link

JE Sayago; RM Ordóñez; MI Isla European Journal of Histochemistry 2009. doi:10.4081/1225

Other claims from this paper (2)

Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

Fructose competitively inhibited invertase.

Taxon: Pteris deflexaPteris deflexat0
Treatment: Fructosee0
Outcome: competitive inhibitorse0

Not reportedComparatorDirection

Verbatim

e0
“Fructose and glucose were competitive and non-competitive inhibitors of the enzyme, respectively.”
✓ located verbatim in the source · abstract, characters 133–230

t0
“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
✓ located verbatim in the source · title, characters 0–90

Title

Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity

J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450

Other claims from this paper (11)

Intervention effect Glucose noncompetitively inhibited invertase.
Intervention effect Proteins suppressed glucose and fructose inhibition of invertase.
Observation The purified invertase was a heterodimer with two reported subunit sizes.
Observation The invertase had beta-fructofuranosidase activity.
Observation The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.
Observation The enzyme hydrolyzed raffinose with a Km of 10.80 mM.
Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
Observation Pinnas had the highest invertase levels.
Observation Invertase was localized mainly in phloem cells.
Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.

Intervention effectobservedoriginal resultnegativemeasured

Claim · model-written summary

Glucose noncompetitively inhibited invertase.

Taxon: Pteris deflexaPteris deflexat0
Treatment: glucosee0
Outcome: non-competitive inhibitorse0

Not reportedComparatorDirection

Verbatim

e0
“Fructose and glucose were competitive and non-competitive inhibitors of the enzyme, respectively.”
✓ located verbatim in the source · abstract, characters 133–230

t0
“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
✓ located verbatim in the source · title, characters 0–90

Title

Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity

J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450

Other claims from this paper (11)

Intervention effect Fructose competitively inhibited invertase.
Intervention effect Proteins suppressed glucose and fructose inhibition of invertase.
Observation The purified invertase was a heterodimer with two reported subunit sizes.
Observation The invertase had beta-fructofuranosidase activity.
Observation The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.
Observation The enzyme hydrolyzed raffinose with a Km of 10.80 mM.
Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
Observation Pinnas had the highest invertase levels.
Observation Invertase was localized mainly in phloem cells.
Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.

Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Proteins suppressed glucose and fructose inhibition of invertase.

Taxon: Pteris deflexaPteris deflexat0
Treatment: proteinse0
Outcome: glucose and fructose inhibitione0
Direction: suppressede0

Not reportedComparator

Verbatim

e0
“proteins suppressed glucose and fructose inhibition of the enzyme”
✓ located verbatim in the source · abstract, characters 237–302

t0
“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
✓ located verbatim in the source · title, characters 0–90

Title

Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity

J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450

Other claims from this paper (11)

Intervention effect Fructose competitively inhibited invertase.
Intervention effect Glucose noncompetitively inhibited invertase.
Observation The purified invertase was a heterodimer with two reported subunit sizes.
Observation The invertase had beta-fructofuranosidase activity.
Observation The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.
Observation The enzyme hydrolyzed raffinose with a Km of 10.80 mM.
Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
Observation Pinnas had the highest invertase levels.
Observation Invertase was localized mainly in phloem cells.
Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.

Observationobservedoriginal resultmeasured

Claim · model-written summary

The purified invertase was a heterodimer with two reported subunit sizes.

Taxon: Pteris deflexaPteris deflexat0
Outcome: heterodimere0
Value: Mr 90,000 Daltonse0
Qualifier: subunits of 66,000 and 30,000 Daltonse0

Verbatim

e0
“The purified enzyme was an heterodimer Mr 90,000 Daltons composed of subunits of 66,000 and 30,000 Daltons.”
✓ located verbatim in the source · abstract, characters 468–575

t0
“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
✓ located verbatim in the source · title, characters 0–90

Title

Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity

J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450

Other claims from this paper (11)

Intervention effect Fructose competitively inhibited invertase.
Intervention effect Glucose noncompetitively inhibited invertase.
Intervention effect Proteins suppressed glucose and fructose inhibition of invertase.
Observation The invertase had beta-fructofuranosidase activity.
Observation The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.
Observation The enzyme hydrolyzed raffinose with a Km of 10.80 mM.
Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
Observation Pinnas had the highest invertase levels.
Observation Invertase was localized mainly in phloem cells.
Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.

Observationobservedoriginal resultmeasured

Claim · model-written summary

The invertase had beta-fructofuranosidase activity.

Taxon: Pteris deflexaPteris deflexat0
Outcome: beta-fructofuranosidase activitye0

Verbatim

e0
“The enzyme had beta-fructofuranosidase activity”
✓ located verbatim in the source · abstract, characters 576–623

t0
“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
✓ located verbatim in the source · title, characters 0–90

Title

Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity

J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450

Other claims from this paper (11)

Intervention effect Fructose competitively inhibited invertase.
Intervention effect Glucose noncompetitively inhibited invertase.
Intervention effect Proteins suppressed glucose and fructose inhibition of invertase.
Observation The purified invertase was a heterodimer with two reported subunit sizes.
Observation The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.
Observation The enzyme hydrolyzed raffinose with a Km of 10.80 mM.
Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
Observation Pinnas had the highest invertase levels.
Observation Invertase was localized mainly in phloem cells.
Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.

Observationobservedoriginal resultmeasured

Claim · model-written summary

The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.

Taxon: Pteris deflexaPteris deflexat0
Outcome: hydrolyzed mainly sucrosee0
Value: 3.22e0

Verbatim

e0
“hydrolyzed mainly sucrose but also raffinose and stachyose, with Km of 3.22, 10.80 and 38.50 mM, respectively.”
✓ located verbatim in the source · abstract, characters 628–738

t0
“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
✓ located verbatim in the source · title, characters 0–90

Title

Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity

J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450

Other claims from this paper (11)

Intervention effect Fructose competitively inhibited invertase.
Intervention effect Glucose noncompetitively inhibited invertase.
Intervention effect Proteins suppressed glucose and fructose inhibition of invertase.
Observation The purified invertase was a heterodimer with two reported subunit sizes.
Observation The invertase had beta-fructofuranosidase activity.
Observation The enzyme hydrolyzed raffinose with a Km of 10.80 mM.
Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
Observation Pinnas had the highest invertase levels.
Observation Invertase was localized mainly in phloem cells.
Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.

Observationobservedoriginal resultmeasured

Claim · model-written summary

The enzyme hydrolyzed raffinose with a Km of 10.80 mM.

Taxon: Pteris deflexaPteris deflexat0
Outcome: raffinosee0
Value: 10.80e0

Verbatim

e0
“hydrolyzed mainly sucrose but also raffinose and stachyose, with Km of 3.22, 10.80 and 38.50 mM, respectively.”
✓ located verbatim in the source · abstract, characters 628–738

t0
“Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity”
✓ located verbatim in the source · title, characters 0–90

Title

Proteinaceous Inhibitor Versus Fructose as Modulators of Pteris deflexa Invertase Activity

J.E. Sayago; M.A. Vattuone; A.R. Sampietro; et al. Journal of Enzyme Inhibition and Medicinal Chemistry 2002. doi:10.1080/14756360290026450

Other claims from this paper (11)

Intervention effect Fructose competitively inhibited invertase.
Intervention effect Glucose noncompetitively inhibited invertase.
Intervention effect Proteins suppressed glucose and fructose inhibition of invertase.
Observation The purified invertase was a heterodimer with two reported subunit sizes.
Observation The invertase had beta-fructofuranosidase activity.
Observation The enzyme hydrolyzed mainly sucrose with a Km of 3.22 mM.
Observation The enzyme hydrolyzed stachyose with a Km of 38.50 mM.
Observation Invertase activity had an optimum pH of 5.0 and occurred in almost every leaf tissue.
Observation Pinnas had the highest invertase levels.
Observation Invertase was localized mainly in phloem cells.
Observation Invertase protein was also found in epidermis, collenchyma and parenchyma cells.