Purification and characterization of α2-macroglobulin from grass carp Ctenopharyngodon idellus: Cloning a segment of the corresponding gene

Li, F.L.; Chen, Lu

doi:10.1016/j.fsi.2005.06.006

Cited by 17 publications

(7 citation statements)

References 12 publications

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“…2), and the determination showed total purification of 47.77 folds with a yield of 28.90%. Li and Lu [12] has also applied the same purificaiton strategy and obtained 2 -M from grass carp (Ctenopharyngodon idellus), but no information on purity and recovery is provided. Due to the inhibitory activities towards papain and trypsin, the inhibitor is tentatively considered as 2 -M. …”

Section: Resultsmentioning

confidence: 99%

“…And because of the outbreak of bovine spongiform encephalopathy and foot-and-mouth disease, food grade inhibitors derived from sources other than cattle and swine are preferred. Recently, 2 -M was purified and characterized from shrimps [9,10], mud crab Scylla serrata [11] and grass carp Ctenopharyngodon idellus [12]. The application of fish protease inhibitors in surimi gel processing was favorable [13].…”

Section: Introductionmentioning

confidence: 99%

“…The application of fish protease inhibitors in surimi gel processing was favorable [13]. Fish plasma contained powerful protease inhibitors such as 2 -M [12,13]. The objective of this study is to purify and characterize 2 -M from Chum Salmon (Oncorhynchus keta) Plasma and to investigate its inhibitory effect on autolysis of myofibrillar proteins from Alaska pollock (Theragra chalcogramma).…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of α<inf>2</inf>-macroglobulin from chum salmon plasma

Duan

Lin

et al. 2011

2011 International Conference on Remote Sensing, Environment and Transportation Engineering

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Chum salmon plasma 2 -macroglobulin ( 2 -M) was first puri ed by polyethylene glycol gradient precipitation, gel ltration and anion-exchange chromatography from chum salmon plasma. The 2 -M was purified 47.77-fold with a yield of 28.90% towards papain. The 2 -M showed molecualr weight (Mw) of 175 kDa and consists of two different subunits of Mw 95 kDa and 80 kDa, respectively. The 2 -M was stable towards papain and trypsin at pH ranges from 5.0 to 8.0, and was thermal stable at temperatures below 50 . The 2 -M was applied to Alaska pollock surimi and was able to inhibit the gel weakening in a concentration-dependent manner.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of α<inf>2</inf>-macroglobulin from chum salmon plasma

Duan

Lin

et al. 2011

2011 International Conference on Remote Sensing, Environment and Transportation Engineering

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“…The expression of A2M in defence against pathogens has been reported in number of fish species i.e. grass carp [4], rainbow trout and brook charr [5], common carp [6], gilthead seabream [7], plaice [8] and brook trout [9].…”

Section: Introductionmentioning

confidence: 99%

Tissue specific alpha-2-Macroglobulin (A2M) splice isoform diversity in Hilsa shad, Tenualosa ilisha (Hamilton, 1822)

et al. 2019

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The present study, for the first time, reported twelve A2M isoforms in Tenualosa ilisha , through SMRT sequencing. Hilsa shad, T . ilisha , an anadromous fish, faces environmental stresses and is thus prone to diseases. Here, expression profiles of different A2M isoforms in four tissues were studied in T . ilisha , for the tissue specific diversity of A2M. Large scale high quality full length transcripts (>0.99% accuracy) were obtained from liver, ovary, testes and gill transcriptomes, through Iso-sequencing on PacBio RSII . A total of 12 isoforms, with complete putatative proteins, were detected in three tissues (7 isoforms in liver, 4 in ovary and 1 in testes). Complete structure of A2M mRNA was predicted from these isoforms, containing 4680 bp sequence, 35 exons and 1508 amino acids. With Homo sapiens A2M as reference, six functional domains (A2M_N,A2M_N2, A2M, Thiol-ester_cl, Complement and Receptor domain), along with a bait region, were predicted in A2M consensus protein. A total of 35 splice sites were identified in T . ilisha A2M consensus transcript, with highest frequency (55.7%) of GT-AG splice sites, as compared to that of Homo sapiens . Liver showed longest isoform (X1) consisting of all domains, while smallest (X10) was found in ovary with one Receptor domain. Present study predicted five putative markers (I-212, I-269, A-472, S-567 and Y-906) for EUS disease resistance in A2M protein, which were present in MG2 domains (A2M_N and A2M_N2), by comparing with that of resistant and susceptible/unknown response species. These markers classified fishes into two groups, resistant and susceptible response. Potential markers, predicted in T . ilisha , placed it to be EUS susceptible category. Putative markers reported in A2M protein may serve as molecular markers in diagnosis of EUS disease resistance/susceptibility in fishes and may have a potential for inclusion in the marker panel for pilot studies. Further, challenging studies are required to confirm the role of particular A2M isoforms and markers identified in immune protection against EUS disease.

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“…As an ancient innate immune molecule, α 2 M widely presents in aquatic animals including fish (Funkenstein, Rebhan, Dyman & Radaelli ), shrimp (Rattanachai, Hirono, Ohira, Takahashi & Aoki ; Lin, Vaseeharan & Chen ), scallop (Ma, Mai, Xu & Liu ) and crab (Vaseeharan, Lin, Ko, Chiou & Chen ). Additionally, the activity of α 2 M was detected in snail (Bender, Fryer & Bayne ), fish (Li & Lu ) and scallop (Shi & Yang ). To date, there is still a lack in information regarding the α 2 M in sea cucumber, one of the marine invertebrate species with high nutritional and medicinal values.…”

Section: Introductionmentioning

confidence: 99%

Identification and functional characterization of first alpha‐2‐macroglobulin in sea cucumbers

et al. 2016

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The broad‐spectrum protease inhibitor alpha‐2‐macroglobulin (α2M) is widely found in vertebrates and invertebrates. However, no research regarding α2M has been described in sea cucumbers to date. In this study, the first sea cucumber α2M named Stmα2M was identified from Stichopus monotuberculatus, a tropical species with high edible and economic values in Southern China. The Stmα2M cDNA is 5276 bp in length, containing a 5′‐untranslated region (UTR) of 279 bp, a 3′‐UTR of 344 bp and an open reading frame of 4653 bp that encodes a protein of 1550 amino acids. The Stmα2M possesses all the three characteristics of known α2M proteins, including the bait region domain, thioester domain and receptor‐binding domain. Higher levels of mRNA expression were noticed in intestine, respiratory tree, coelomocytes and tentacle of S. monotuberculatus. Transcriptional expression of Stmα2M showed the strongest response to lipopolysaccharides (LPS, 8.19‐fold up‐regulation) after 6 h post‐challenge in coelomocytes. In addition, the α2M activity was detected in S. monotuberculatus and protein activity of α2M increased remarkably at 6 h after LPS stimulation. As a whole, this study indicated that Stmα2M is an important immune‐related molecule, and the study on functions of Stmα2M may provide some new and valuable ideas for preventing and controlling diseases of cultured sea cucumbers.

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Purification and characterization of α2-macroglobulin from grass carp Ctenopharyngodon idellus: Cloning a segment of the corresponding gene

Cited by 17 publications

References 12 publications

Purification and characterization of α<inf>2</inf>-macroglobulin from chum salmon plasma

Purification and characterization of α<inf>2</inf>-macroglobulin from chum salmon plasma

Tissue specific alpha-2-Macroglobulin (A2M) splice isoform diversity in Hilsa shad, Tenualosa ilisha (Hamilton, 1822)

Identification and functional characterization of first alpha‐2‐macroglobulin in sea cucumbers

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Purification and characterization of α2-macroglobulin from grass carp Ctenopharyngodon idellus: Cloning a segment of the corresponding gene

Cited by 17 publications

References 12 publications

Purification and characterization of &#x03B1;<inf>2</inf>-macroglobulin from chum salmon plasma

Purification and characterization of &#x03B1;<inf>2</inf>-macroglobulin from chum salmon plasma

Tissue specific alpha-2-Macroglobulin (A2M) splice isoform diversity in Hilsa shad, Tenualosa ilisha (Hamilton, 1822)

Identification and functional characterization of first alpha‐2‐macroglobulin in sea cucumbers

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Purification and characterization of α<inf>2</inf>-macroglobulin from chum salmon plasma

Purification and characterization of α<inf>2</inf>-macroglobulin from chum salmon plasma