Inga cylindrica 9 claims

species · family Fabaceae · green plant · NCBI Taxonomy ↗

NCBI synonyms: Mimosa cylindrica

2 spellings

Inga cylindrica
Inga cylindricaDouglas · CC BY 4.0 · iNaturalist ↗
Observationobservedoriginal resultmeasured

Claim · model-written summary

Linolenic acid was the dominant fatty acid component in seeds of Inga cylindrica.

Taxon
Inga cylindricaInga cylindricae6
Outcome
linolenic acide6
Qualifier
dominant componente6

Verbatim

e6

“linolenic acid was the dominant component in Inga cylindrica”

✓ located verbatim in the source · abstract, characters 1408–1468

Title

Anemochorous and zoochorous seeds of trees from the Brazilian savannas differ in fatty acid content and composition

Augusto Cesar Franco; Risolandia Bezerra de Melo; Cristiane Silva Ferreira; et al. AoB Plants 2023. doi:10.1093/aobpla/plad042

Other claims from this paper (10)
Observationobservedoriginal resultpositivemeasured

Claim · model-written summary

I. cylindrica was highlighted for high protein value.

Taxon
I. cylindricaInga cylindricae0
Outcome
high protein valuee0

Verbatim

e0

“especially the P. floribundum, I. cylindrica, and P. gonoacantha for their high protein value”

✓ located verbatim in the source · abstract, characters 1077–1170

Title

Nutrient composition of some important Brazilian savanna trees and their potential for animal feed

Carlos de Melo e Silva Neto; Paulo Vitor Divino Xavier de Freitas; Iara Jaime de Pina; et al. Australian Journal of Crop Science 2022. doi:10.21475/ajcs.22.16.03.p3564

Other claims from this paper (3)
Observationobservedoriginal resultmeasured

Claim · model-written summary

ICTI was purified as a single polypeptide chain from Inga cylindrica seeds.

Taxon
Inga cylindricaInga cylindricae0
Organ / stage
seedse0
Gene
Inga cylindrica Trypsin Inhibitor (ICTI)e0
Outcome
single polypeptide chaine0

Verbatim

e0

“Inga cylindrica Trypsin Inhibitor (ICTI) was purified as a single polypeptide chain by one step anion-exchange chromatography from a crude extract of Inga cylindrica (Vell.) Mart. seeds.”

✓ located verbatim in the source · abstract, characters 0–186

Title

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Leonardo A Calderon; Humberto A Almeida Filho; Rozeni C. L Teles; et al. Brazilian Journal of Plant Physiology 2010. doi:10.1590/s1677-04202010000200001

Other claims from this paper (6)
Observationobservedoriginal resultmeasured

Claim · model-written summary

ICTI has a mass of 19.5 kDa.

Taxon
Inga cylindricaInga cylindricae1
Gene
ICTIe0
Outcome
proteine0
Value
19.5 kDae0

Verbatim

e0

“ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM).”

✓ located verbatim in the source · abstract, characters 187–309
e1

“Inga cylindrica Trypsin Inhibitor (ICTI)”

✓ located verbatim in the source · abstract, characters 0–40

Title

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Leonardo A Calderon; Humberto A Almeida Filho; Rozeni C. L Teles; et al. Brazilian Journal of Plant Physiology 2010. doi:10.1590/s1677-04202010000200001

Other claims from this paper (6)
Observationobservedoriginal resultmeasured

Claim · model-written summary

ICTI inhibits bovine trypsin with Ki of 4.3 nM.

Taxon
Inga cylindricaInga cylindricae1
Gene
ICTIe0
Outcome
inhibitory activity against bovine trypsine0
Value
4.3 nMe0

Verbatim

e0

“ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM).”

✓ located verbatim in the source · abstract, characters 187–309
e1

“Inga cylindrica Trypsin Inhibitor (ICTI)”

✓ located verbatim in the source · abstract, characters 0–40

Title

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Leonardo A Calderon; Humberto A Almeida Filho; Rozeni C. L Teles; et al. Brazilian Journal of Plant Physiology 2010. doi:10.1590/s1677-04202010000200001

Other claims from this paper (6)
Observationobservedoriginal resultmeasured

Claim · model-written summary

ICTI is a beta type protein with reported strand, turn and helix proportions.

Taxon
Inga cylindricaInga cylindricae1
Gene
ICTIe1
Outcome
β type proteine0
Qualifier
40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helixe0

Verbatim

e0

“this inhibitor is a β type protein (40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helix) in accordance with properties displayed in Kunitz type inhibitors.”

✓ located verbatim in the source · abstract, characters 352–510
e1

“Inga cylindrica Trypsin Inhibitor (ICTI)”

✓ located verbatim in the source · abstract, characters 0–40

Title

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Leonardo A Calderon; Humberto A Almeida Filho; Rozeni C. L Teles; et al. Brazilian Journal of Plant Physiology 2010. doi:10.1590/s1677-04202010000200001

Other claims from this paper (6)
Observationobservedoriginal resultmeasured

Claim · model-written summary

ICTI had its highest thermal stability at pH 7.0 within pH 1.6 to 10.0.

Taxon
Inga cylindricaInga cylindricae1
Gene
ICTIe0
Outcome
highest stabilitye0
Value
70.0 ºCe0
Qualifier
pH 7.0e0

Verbatim

e0

“ICTI is a thermal stable protein within a wide range of pH (1.6 to 10.0) exhibiting highest stability at pH 7.0 as indicated by Tm of 70.0 ºC and ΔG25 of 48.5 ± 0.7 kJ.mol-1.”

✓ located verbatim in the source · abstract, characters 511–685
e1

“Inga cylindrica Trypsin Inhibitor (ICTI)”

✓ located verbatim in the source · abstract, characters 0–40

Title

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Leonardo A Calderon; Humberto A Almeida Filho; Rozeni C. L Teles; et al. Brazilian Journal of Plant Physiology 2010. doi:10.1590/s1677-04202010000200001

Other claims from this paper (6)
Observationobservedoriginal resultmeasured

Claim · model-written summary

ICTI had reduced structural stability at pH 1.6 and 10.0.

Taxon
Inga cylindricaInga cylindricae1
Gene
ICTIe1
Outcome
structural stabilitye0
Direction
reducede0
Qualifier
pH 1.6e0

Verbatim

e0

“The values of ΔG25 at pH 1.6 (22.5 ± 1.2 kJ.mol-1) and pH 10.0 (31.5 ± 1.0 kJ.mol-1) indicate a reduced structural stability of the protein under these conditions.”

✓ located verbatim in the source · abstract, characters 686–849
e1

“Inga cylindrica Trypsin Inhibitor (ICTI)”

✓ located verbatim in the source · abstract, characters 0–40

Title

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Leonardo A Calderon; Humberto A Almeida Filho; Rozeni C. L Teles; et al. Brazilian Journal of Plant Physiology 2010. doi:10.1590/s1677-04202010000200001

Other claims from this paper (6)
Mechanismhypothesisoriginal resultmeasured

Claim · model-written summary

The authors attribute pH dependent stability to side chain pKa and folded-state noncovalent interactions.

Taxon
Inga cylindricaInga cylindricae1
Outcome
changes in the non-covalent interactions in the folded statee0
Qualifier
pKa differences of the acid and basic side chainse0

Verbatim

e0

“This is likely to result from pKa differences of the acid and basic side chains reflecting the changes in the non-covalent interactions in the folded state.”

✓ located verbatim in the source · abstract, characters 850–1006
e1

“Inga cylindrica Trypsin Inhibitor (ICTI)”

✓ located verbatim in the source · abstract, characters 0–40

Title

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Leonardo A Calderon; Humberto A Almeida Filho; Rozeni C. L Teles; et al. Brazilian Journal of Plant Physiology 2010. doi:10.1590/s1677-04202010000200001

Other claims from this paper (6)