Analysis Efficiency Marketing System of Fresh Layang Fish (Decapterus Russeli) on Pelabuhan Fish Auction Place in Tegal City

Marketing is an important aspect in running fishing business because it is an economic activity that influences the fluctuation of fishermen\u27s income. The production can be useless if the price is low, thus, marketing has to be good and efficient. This research is about the efficiency of the marketing system of fresh fish layang (Decapterus russeli) in the fish auction place. Specifically, this research is to know : 1) the marketing system of fresh fish layang in Tegal City. 2) the marketing margin of fresh fish layang in Tegal City. 3) the distribution flow of fresh fish layang in Tegal City. 4) the reason fishermen sell their products in the Fish Auction Place. The method use in this research is descriptive analysis method, The registration data and literature study. Based on the analysis, it is known that the marketing system of fresh in the Fish Auction Place, seen from the marketing cost calculation, purchasing price, selling price and profit is < 1, which means efficient. And if seen from the marketing margin, the most efficient flow is channel 4 (the 4th channel). Meanwhile, the reason why fishermen sell their Fish Auction Place is because of the guarantee that their product will be sold. Fish is a product that is easily broken and rotten. Therefore, the guarantee that the product will be sold, can minimize loss risk for fisherman

Additional file 3: of Identification of host cellular proteins that interact with the M protein of a highly pathogenic porcine reproductive and respiratory syndrome virus vaccine strain

Table S3. The list of the enriched KEGG Pathways of the PRRSV M protein interacting proteins. (XLS 277 kb

Identification of the mAb 3D7 epitope by Western blot.

<p>Western blot analysis of GST-HuN4-F112/F5-N fusion proteins with the mAb 3D7 (A). Lane 1: ultracentrifugal HuN4-F112; lane 2: GST-HuN4-F112-N; lane 3: GST-HuN4-F5-N; lane 4: GST. Truncated fragments were detected with the mAb 3D7 (B). The mAb 3D7 specifically reacted with N protein fragment NF1-3-2 (amino acids 7–33) after three rounds of truncation. F1B is the fragment (amino acids 10–33) identified previously as not recognized by the mAb 3D7 (data not shown), used here as a negative control.</p

Reactivity of mAbs 3D7 (B) and 1F10 (C) with HP-PRRSV HuN4 and vaccine strains in Marc-145 cells and transiently transfected 293T cells expressing expressing N and GP3 proteins.

<p>HuN4-F112 (attenuated in our laboratory), JXA1-R, and TJM-F92 are commercial vaccines used in China. HuN4, HNZJJ, and HLJMZ are HP-PRRSVs isolated by our laboratory. The two mAbs 3D7 and 1F10 recognized N and GP3 protein expressed by transiently transfected cells. 293T cells pCAGGS-transfected were used as a negative control. Marc-145 cells infected by PRRSV staining with the mAb 3F7 and 293T cells pCAGGS-N/GP3-transfected staining with the mAbs 2E9 and 4G5 were used as positive controls (A). Magnification 200×.</p

Reactivity of the mAb 3D7 (B) with two HP-PRRSV strains at different passages.

<p>The mAb 3D7 reacted with HuN4-F9/F17 and HLJMZ-F3/F4 passages. The mAb 3F7 (A) was used as a positive control.</p

The truncated GP3 fragments (A) and the pursue absence GP3-63-77aa fragments (B) were identified by Western blot with the anti-GST mAb, the mAb 1F10, and positive sera.

<p>(A) M: protein marker; 1: GST-GP3-1-171aa; 2: GST-GP3-41-100aa; 3: GST-GP3-41-55aa; 4: GST-GP3-56-70aa; 5: GST-GP3-48-62aa; 6: GST-GP3-63-77aa; 7: GST. (B) M: protein marker; 1: GST-GP3-63-76aa; 2: GST-GP3-63-75aa; 3: GST-GP3-63-74aa; 4: GST-GP3-63-73aa; 5: GST-GP3-63-72aa; 6: GST-GP3-63-71aa; 7: GST-GP3-64-77aa; 8: GST-GP3-65-77aa; 9: GST-GP3-66-77aa; 10: GST-GP3-67-77aa; 11: GST-GP3-68-77aa; 12: GST-GP3-69-77aa; 13: GST-GP3-70-77aa; 14: GST-GP3-68-76aa; 15: GST-GP3-69-76aa. The deduced epitope (69-76aa) was vertified not to be a true one, while the motif (68-76aa) was the epitope recognized by the mAb 1F10. But the epitope was not recognized by positive sera. The positive sera 4^# and 7^# were pig hyperimmune sera with high titer of neutralizing antibodies against HP-PRRSV, which were obtained from pigs immunized by HuN4-F112 once and then inoculated with HP-PRRSV HuN4 virulent strain (HuN4-F5) three times. The positive serum 28^# was collected from a pig inoculated with HP-PRRSV HuN4 virulent strain (HuN4-F5) at 14DPI. A pig was immunized with HuN4-F112 and then inoculated with HP-PRRSV HuN4 virulent strain (HuN4-F5) at 21DPI, the positive serum 71^# was collected from the pig after 3 weeks.</p

Multiple sequence alignments of the epitopes of the N and GP3 proteins of HP-PRRSV, classical PRRSV isolates, and vaccine strains.

<p>The amino acid sequences of the epitopes identified are underlined. The strains in square frame are sequenced in our laboratory. Strigulas (red square frame) stands in for the amino acids deleted from the North American PRRSV relative to the sequence of European virus. The amino acid sequences are aligned using the DNAstar MegAlign software.</p

Primer sets for the amplification of the ORF3 gene and its truncated fragments.

<p>In the F112-GP3 primers, the forward and reverse primers contain <i>Bam</i>HI and <i>Xho</i>I recognition sites, respectively (underlined). Other oligomeric nucleic acid fragments were annealed directively and be used for amino acids pursue absence, which also contain <i>Bam</i>HI and <i>Xho</i>I recognition sites (underlined). Bold font indicates termination codons.</p><p>Primer sets for the amplification of the ORF3 gene and its truncated fragments.</p

PRRSV strains cited in this study.

<p>PRRSV strains cited in this study.</p