• Title/Summary/Keyword: caeca

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Isolation of a starfish myorelaxant peptide (SMP) isotype from the pyloric caeca of Patiria pectinifera

  • Kubarova, Anastasia;Go, Hye-Jin;Park, Nam Gyu
    • Fisheries and Aquatic Sciences
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    • v.24 no.4
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    • pp.163-170
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    • 2021
  • Peptides are naturally occurring biological molecules that are found in all living organisms. These biologically active peptides play a key role in various biological processes. The aim of this study is the extraction and the purification of bioactive materials that induce relaxation of an apical muscle from the pyloric caeca of Patiria pectinifera. The acidified pyloric caeca extract was partially separated by the solid phase extraction using a stepwise gradient on Sep-Pak C18 cartridge. Among the fractions, materials eluted with 60% methanol/0.1% trifluoroacetic acid was put a thorough of a series of high performance liquid chromatography (HPLC) steps to isolate a neuropeptide with relaxation activity. The purified compound was eluted at 28% acetonitrile in 0.1% trifluoroacetic acid with retention time of 25.8 min on the CAPCELL-PAK C18 reversed-phase column. To determine the molecular weight and the amino acid sequence of the purified peptide, LC-MS and Edman degradation method were used, respectively. The primary structure of the peptide was determined to be FGMGGAYDPLSAGFTD which corresponded to the amino acid sequence of a starfish myorelaxant peptide (SMP) isotype (SMPb) found in the cDNA sequence encoding SMPa and its isotypes. In this study, a muscle relaxant neuropeptide (SMPb) has been isolated from pyloric caeca of starfish P. pectinifera. This is the first report of SMPb isolation on the protein level from P. pectinifera.

Studies on the Fine Structure of Caeca in Domestic Geese

  • Chen, Yieng How;Hsu, Hoang Kao;Hsu, Jenn Chung
    • Asian-Australasian Journal of Animal Sciences
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    • v.15 no.7
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    • pp.1018-1021
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    • 2002
  • The objective of this study was to investigate the villus distribution in the caeca of domestic geese based on the fine structure. The caeca of White Roman geese, 14-week old, were sampled and specimens were detected under photomicroscope and scanning electron microscope (SEM). The results indicated that the villi existed at the proximal caecum. The morphologies of these villi showed finger-like, peak-like or tongue-like shapes. The heights of the villi decreased far from the proximal caecum. No villi were found in the middle and distal caecum. It was obvious that the proximal segment was the main portion for absorbing food nutrients in the caeca. The caecal content particles were small and possessed a viscid character. The large particles filtered out at the proximal caecum just like a mesh. The surface of the middle caecum exhibited parallel ridges with no villi. There were band plicae circular shapes found in the middle caecum under scanning electron microsopy.

Purification of Two Novel Antimicrobial Peptides from Pyloric Caeca of the Starfish Asterina pectinifera (별불가사리 Asterina pectinifera의 유문맹낭 추출물로부터 새로운 2종류의 항균활성 펩타이드의 정제)

  • Go, Hye-Jin;Bae, Yun Jung;Park, Nam Gyu
    • Journal of Life Science
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    • v.24 no.8
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    • pp.860-864
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    • 2014
  • PAP-1, a novel antimicrobial peptide isolated from pyloric caeca extract of the starfish Asterina pectinifera was purified and characterized. First, the acidified pyloric caeca extract was put through Sep-Pak C18 solid phase extraction cartridge using a stepwise gradient. Among the eluents, RM 60 (retained materials at 60% methanol) showed good antimicrobial activity against Bacillus subtilis and Escherichia coli D31 and was purified in C18 reversed-phase and ion-exchange high-performance liquid chromatography columns. The purification steps yielded two novel peptides showing strong antimicrobial activities. These peptides were named pyloric caeca A. pectinifera peptide 1 and 2 (PAP-1 and PAP-2). For the characterization of the purified peptides, the molecular weights and amino acid sequences were determined by MALDI-TOF MS and Edman degradation. The molecular weights of PAP-1 and PAP-2 were about 2951.54 Da and 2980.15 Da respectively. The amino acid sequences of PAP-1 and PAP-2 were partially determined: AIQNAGES and AIQNAAES, respectively. PAP-2 is an isoform of PAP-1, differing merely by a single residue at position 6 (glycine or alanine). The comparison of the N-terminal amino acid sequences and molecular weights of the peptides with those of other known antimicrobial peptides revealed that PAP-1 and PAP-2 have no homology with any known peptides. These findings suggest that PAP-1 and PAP-2 play a significant role in the innate defense system of starfish pyloric caeca.

Benthic Fauna on the Hangang Estuary (한강 하구역의 저서동물상)

  • Kil Hyun Jong;Rho Hyun Soo;Paik Sang-Gyu;Song Sung Joon;Choe Byung Lae;Kim Won
    • Korean Journal of Environmental Biology
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    • v.23 no.3 s.59
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    • pp.250-256
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    • 2005
  • A benthic faunal survey of the Hangang Estuary located in the northwestern part of South Korea was performed in October 2004. A total of 11 species identified, which were comprised of two species of molluscs bivalves (Limnoperna fortunei and Corbicula felnouilliana) in two families, two species of annelids polychaetes (Neanthes japonica and Nephtys caeca) in two families, and seven species of decapods (Palaemon carinicauda, P. annandalei, P. modestus, Ilyoplax deschampsi, Eriocheir sinensis, Eriocheir leptognathus and Sesarma dehaani) in four families. Four of the 11 species in six families, Limnoperna fortunei, Neanthes japonica, Nephtys caeca and Palaemon modestus, were newly found in this study area. Eleven species were presently listed with brief ecological remarks.

The Proteinase Distributed in the Intestinal Organs of Fish 1. Purification of the Three Alkaline Proteinases from the Pyloric Caeca of Mackerel, Scomber japonicus (어류의 장기조직에 분포하는 단백질분해효소에 관한 연구 1. 고등어 유문수조직으로부터 3종의 알칼리성 단백질분해효소의 분리${\cdot}$정제)

  • PYEUN Jae-Hyeung;KIM Hyeung-Rak
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.19 no.6
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    • pp.537-546
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    • 1986
  • In the previous paper(Kim et al, 1986), the alkaline proteinase from the pyloric caeca of mackerel was shown relatively strong activity in the alkaline pH range. Therefore purification of the enzyme has been undertaken to identify the proteolytic enzyme and three alkaline proteinases were isolated by ammonium sulfate fractionation, DEAE-Sephadex A-50 column chromatography and Sephadex G-100 gel filtration. One percent sodium chloride solution was the most effective for the extraction of alkaline proteinase from the pyloric caeca of mackerel. Three alkaline proteinases temporarily designated Enz. A, B and C were isolated from the pyloric caeca of mackerel, and identified to be homogeneous with electrophoresis. The specific activity of the purified Enz. A, B and C was increased to 34, 53 and 37-fold over the crude enzyme solution, respectively. Yield of them was 1.6, 2.1 and $1.5\%$, respectively, and a combined yield was $5.2\%$.

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Influence of Caecectomy on the Bioavailability of Minerals from Vegetable Protein Supplements in Adult Roosters

  • Vasan, P.;Dutta, Narayan;Mandal, A.B.;Sharma, K.
    • Asian-Australasian Journal of Animal Sciences
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    • v.21 no.8
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    • pp.1178-1182
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    • 2008
  • The present study was designed to assess the influence of caeca on the availability of calcium, phosphorus, magnesium, manganese and copper from soybean, sunflower, rapeseed, sesame, fish and meat cum bone meal in adult roosters. The excretion of endogenous origin minerals viz., copper, magnesium, manganese and calcium was significantly (p<0.001) higher in caecectomized than in normal roosters. The difference in the endogenous excretion was 50; 60.45; 40.35 and 29.63 per cent for copper, magnesium, manganese and calcium, respectively, in caecectomized roosters. The caeca played a pivotal role in the reabsorption of endogenous origin calcium, magnesium, manganese and copper. The mechanism of phosphorus absorption by the caecal epithelium was negligible. The caecectomized roosters underestimated the bioavailability of copper in sunflower meal and manganese in almost all the test feedstuffs. The present investigation revealed that the caeca played a critical role in the absorption of minerals from vegetable protein feedstuffs which escape digestion and absorption in the small and large intestinal segments.

A Technique for Caecostomy in the Chicken (닭에 있어서의 Caecostomy (맹장으로 튜브를 삽입하는) 기술)

  • Son, Jang-Ho
    • Journal of Life Science
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    • v.14 no.4
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    • pp.537-540
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    • 2004
  • A caecostomy technique (surgery for inserting tube into caeca) was developed to quantify urine backflow into the caeca. Two days post-surgery, caecostomised chickens were flushed with 20 ml of warm saline solution every other day for 10 days. After surgery birds temporarily lost appetite and activity, but they were restored gradually in a few days. The incision healed within 10 days post-surgery. Excreta were collected daily from caecal tubing and cloaca by surgical attachment of polyethylene collection vessels to the chickens. Post-mortem examinations ascertained that the caeca were intact around the Latex tubing.

Biological Study on the Increment of Survival Rate during Early Life Cycle in the Rockfish, Sebastes schlegeli(Teleostei: Scorpaenidae) - III. Ultrastructure of the Adult Digestive Tract (조피볼락, Sebastes schlegeli의 초기 생활사 동안 생존율 향상을 위한 생물학적 연구 - III. 성체 소화관의 미세구조)

  • Chin, Pyung;Lee, Jung-Sick;Shin, Yun-Kyung;Kim, Hak-Gyoon
    • Korean Journal of Ichthyology
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    • v.10 no.1
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    • pp.115-127
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    • 1998
  • The digestive tract of the rockfish, Sebastes schlegeli composed of pharynx, esophagus, stomach, intestine, anus and ten or eleven pyloric caeca. Pyloric caeca is blind sac of banana shape, and that is originated from pyloric portion of the stomach. The relative length of gut(RLG), that is length of digestive tract to standard length, is about 1.56(n=10). Esophageal muscularis consists of thin outer layer of longitudinal muscle and thick inner layer of circular muscle. Mucosal epithelium consists of columnar epithelium with short microvilli and contains numerous mucous secretory cell. The mucosal folds of the stomach are regular, and the muscularis consists of longitudinal, oblique and circular muscle layer. The chief cell of the gastric gland have a tubular mitochondria, endoplasmic reticula and numerous secretory granules in electron-dense. However, parietal cell contains small mitochondria, endoplasmic reticula and vacuoles in low electron density. Mucosal epithelium of the pyloric caeca and intestine composed of columnar epithelium, goblet cell, rodlet cell and dark cell. Columnar absorptive cell in the pyloric caeca and intestine contains well developed mitochondria, endoplasmic reticula, vesiculated granules in high electron density, pinocytotic vesicles and multivesicular body. Rodlet cell have a well developed cytoplasmic capsule and the endoplasmic reticula in the cytoplasm. Dark cell showing a high electron density in the cytoplasm and contains well developed mitochondria. Columnar epithelium of the intestine have a well developed intercellular junction and the microvilli which contains actin filament originated from the cytoplasm. Mucosal epithelium of the intestine have a longer microvilli and more abundant goblet cells than in the pyloric caeca.

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Effect of Caecectomy on Body Weight Gain, Intestinal Characteristics and Enteric Gas Production in Goslings

  • Chen, Yieng-How;Wang, Shu-Yin;Hsu, Jenn-Chung
    • Asian-Australasian Journal of Animal Sciences
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    • v.16 no.7
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    • pp.1030-1034
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    • 2003
  • Two experiments of four-week duration were conducted to investigate the effect of caecectomy on the intestinal characteristics, body weight gain and gas production in the caeca of White Roman goslings. In experiment I, forty eight 2-wk-old female goslings with similar body weight were randomly divided into four treatments: sham (SHAM), left side caecum removed (LSCR), right side caecum removed (RSCR) and both caeca removed (CAECECTOMY). Smimilarly, experiment II was conducted with twelve 5-wkold male goslings in two treatments: SHAM and CAECECTOMY. Free choice water with ad libitum feed was provided during experiment. At the end of experiment I, goslings were sacrificed and gut length and weight were determined. At 7 and 9 wks of age, birds in experiment II were subjected to respiration calorimetry studies. In both experiments, final body weights were not affected by caecectomy. Results of experiment I indicated that caecectomy did not significantly affect the relative weight (g/100 g BW) of gizzard, small intestine, rectum and colon (p>0.05); however, the relative length of colon and rectum did increase (p<0.05). The remaining caecum did not show compensatory growth in both LSCR and RSCR treatments. In experiment II, results indicated that the average enteric methane production from the caecetomised goslings was significantly lower than that from the bird in SHAM goslings (p<0.05). In comparison with SHAM goslings, calorific loss from entric methane in caecetomised birds was lower (p<0.05). There was no effect of age on methane production. The enteric nitrous oxide production in caeca of goslings was very low with no significantly different between two treatments.

The Proteinase Distributed in the Intestinal Organs of Fish 3. Purification and Some Enzymatic Properties of the Alkaline Proteinases from the Pyloric Caeca of Skipjack, Katsuwonus vagans

  • PYEUN Jae-Hyeung;KIM Hyeung-Rak;HEU Min-Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.21 no.2
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    • pp.85-96
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    • 1988
  • Purification and some properties of alkaline proteinases in the pyloric caeca of skipjack, Katsuwonus vagans, were investigated. Four alkaline proteinases, temporarily designated proteinases I, II, III and IV, were identified from the tissue extract of the pyloric caeca by ammonium sulfate fractionation, DEAE-Sephadex A-50 chromatography, and Sephadex G-100 and G-200 gel filtration. Result of disc-polyacrylamide gel electrophoretic analysis showed that the purified proteinases II and III were homogenous with the yields of $1.5\%\;and\;1.2\%$, and those specific activities were increased to 33 to 37 fold over that of the crude enzyme solution, respectively. Molecular weight of the proteinases II and III determined by sephadex G-100 gel filtration were 28,500 and 24,200, respectively. The optimum conditions for the caseinolytic activity of the two enzymes were pH 9.6 and $48^{\circ}C$. The reaction rates of the two alkaline proteinases were constant to the reaction time to 80 min in the reaction mixture of $3.4{\mu}g/ml$ of enzyme concentration and $2\%$ casein solution. The Km values against casein substrate determined by the method of Lineweaver-Burk were $0.56\%$ for proteinase II and $0.30\%$ for proteinase II. The proteinases II and III were inactivated under the presence of $Ag^+,\;Hg^{2+},\;Ni{2+},\;Fe^{2+},\;and\;Cu^{2+}$, and but activated by $Mn^{2+}\;and\;Ca^{2+}$ and markedly inhibited by the soybean trypsin inhibitor and N-p-toluenesulfonyl-L-lysine chloromethyl ketone. Therefore, the proteinases II and III were found to be a group of serine proteases and assured to be trypsin-like proteinases.

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