Evidence map›Paper›PMID 22101803›Full record

ArticleThe protein journal2012

The effects of temperature and pH on secondary structure and antioxidant activity of Crocodylus siamensis hemoglobin.

Jinda Jandaruang, Jaruwan Siritapetawee, Kanjana Thumanu, Chomphunuch Songsiriritthigul, Chartchai Krittanai, Sakda Daduang, Apisak Dhiravisit, Sompong Thammasirirak

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In one paragraph

Article in The protein journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.9field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 39 citations in OpenAlex.

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  12. Antimicrobial peptides in reptiles.Pharmaceuticals (Basel, Switzerland) · 2014
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Jinda JandaruangFaculty of Science, Department of Biochemistry, Khon Kaen University, Khon Kaen, 40002, Thailand.
Jaruwan Siritapetawee
Kanjana Thumanu
Chomphunuch Songsiriritthigul
Chartchai Krittanai
Sakda Daduang
Apisak Dhiravisit
Sompong Thammasirirak
Khon Kaen University · THSynchrotron Light Research Institute · THMahidol University · THSuranaree University of Technology · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crocodylus siamensis hemoglobin (cHb) was purified by gel filtration chromatography and visualized by SDS-PAGE. Effects of temperature and pH on secondary structure and conformation changes of cHb were studied using circular dichroism spectropolarimeter and fourier transform infrared spectrophotometer. The secondary structure of intact cHb was mainly α-helices. cHb was not heat stable when heated at 65 °C and cooled down to original temperature, indicating the irreversible unfolding process. The stability of cHb at different pH ranging from 2.5 to 10.5 was determined. The maximum value of the α-helix content was found at pH 3.5 and tended to decrease at strong acid and strong base. The antioxidant activities of heat treated cHb and cHb in solution with pH range 2.5 to 10.5 were tested by DPPH radical scavenging assay. cHb at pH 4.5, having highest β-turn structure, showed highest radical scavenging activity. In contrast to pH, heat had no effect on antioxidant activity of cHb.

Indexed as

Alligators and CrocodilesAnimalsAntioxidantsHemoglobinsHydrogen-Ion ConcentrationProtein StabilityProtein Structure, TertiaryTemperatureAntioxidantsHemoglobins

Identifiers

PMID22101803
OpenAlexW1966109979

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.