<?xml version="1.0" encoding="UTF-8"?>
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  <title>DSpace Collection: Bachelor thesis of BS Biology students</title>
  <link rel="alternate" href="http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/170" />
  <subtitle>Bachelor thesis of BS Biology students</subtitle>
  <id>http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/170</id>
  <updated>2026-05-12T10:08:52Z</updated>
  <dc:date>2026-05-12T10:08:52Z</dc:date>
  <entry>
    <title>Cloning and Transformation of Salmonella typhi Flagellin Gene in the Yeast Expression Vector pPICZaA</title>
    <link rel="alternate" href="http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3691" />
    <author>
      <name>Ramos, Krzcht Odessa D.M.</name>
    </author>
    <author>
      <name>Reyes, Elwilynne Q.T.</name>
    </author>
    <id>http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3691</id>
    <updated>2026-05-11T19:01:46Z</updated>
    <published>2005-04-01T00:00:00Z</published>
    <summary type="text">Title: Cloning and Transformation of Salmonella typhi Flagellin Gene in the Yeast Expression Vector pPICZaA
Authors: Ramos, Krzcht Odessa D.M.; Reyes, Elwilynne Q.T.
Abstract: Increased resistance to antibiotics and inefficient vaccines&#xD;
prompted the development of new vaccines against the typhoid bacterium&#xD;
Salmonella typhi. The object of the study was to clone and transform the&#xD;
antigenic hypervariable regions IV to VI of the S. typhi flagellin gene in&#xD;
the yeast expression vector pPICZaA, which will facilitate the production&#xD;
of stable recombinant yeast cells for the formulation of new vaccines.&#xD;
Plasmid pGTE-PCRII p23 containing the flagellin gene fragment and&#xD;
pPICZaA were isolated from Escherichia coli strain JM-109 and then&#xD;
subjected to restriction enzyme analysis using EcoRI/Xbal. The identified&#xD;
flagellin gene fragment was ligated to the yeast expression vector&#xD;
pPICZaA and the new construct was transformed into the E. coli strain&#xD;
DH5a. The transformants were selected based on their resistance to the&#xD;
antibiotic ZeocinTM and analyzed by restriction enzyme digestion with&#xD;
BgnI, EcoRI/Xbal, and HindIII/EcoRI. The new constructs, designated as&#xD;
pEO, were confirmed to be of the expected size - approximately equal to&#xD;
4.1 kb. The pEO plasmids were isolated and transformed into the Pichia&#xD;
pastoris strain X-33 through electroporation (5 milliseconds at 1.5 kV)&#xD;
and the lithium chloride method. However, transformation in P. pastoris&#xD;
was unsuccessful. This may be due to one or several factors, such as&#xD;
technical and procedural errors.</summary>
    <dc:date>2005-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>A Taxonomic Survey of a Seagrass Community in the Northern Coast of Semirara Island, Antique</title>
    <link rel="alternate" href="http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3680" />
    <author>
      <name>Cedo, Joseph Paulo M.</name>
    </author>
    <id>http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3680</id>
    <updated>2026-05-06T19:02:39Z</updated>
    <published>1999-03-01T00:00:00Z</published>
    <summary type="text">Title: A Taxonomic Survey of a Seagrass Community in the Northern Coast of Semirara Island, Antique
Authors: Cedo, Joseph Paulo M.
Abstract: The dwindling stature of the ecosystem of today has drawn&#xD;
attention to its neglected aspects. It is only now that&#xD;
people are learning the importance of the seagrass&#xD;
community. The coexistence of Organisms in the estuarine&#xD;
regions has laid a bigger importance on seagrasses, thus,&#xD;
prompting this research. Using three transect lines of 100&#xD;
meters in length each; a taxonomic survey of the seagrass&#xD;
community in the Northern Coast of Semirara Island,&#xD;
Antique was done. The results of the study show that after&#xD;
having computed for the Shannon's Diversity Index, the&#xD;
index was highest for seagrass (0.6393) while lowest for&#xD;
alga (0.3003). In Site C, the index was lowest for seagrass&#xD;
(0.2788), while highest for alga (0.4369). Likewise, it can&#xD;
be noted that the following species of seagrasses can be&#xD;
found in the sites: Enhalus acoroides, Cymodocea&#xD;
rotunda/a, Cymodocea sp., Halodule pinifolia, Halodule&#xD;
sp., and Halophila ovalis. Meanwhile, the following&#xD;
species of algae were found: Halimeda macroloba,&#xD;
Halimeda sp., Valonia sp., Galaxaura sp., and Dictyota&#xD;
sp. The seagrass community can be characterized by the&#xD;
dominant species, which is the Cymodecea rotundata.</summary>
    <dc:date>1999-03-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Schistosoma Mansoni and S. Japonicum Cross-Reactive Antigens: Potential Candidate Molecules for a Universal Vaccine</title>
    <link rel="alternate" href="http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3676" />
    <author>
      <name>Abacan, Mary Ann R.</name>
    </author>
    <author>
      <name>Receno, Pia Angela O.</name>
    </author>
    <id>http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3676</id>
    <updated>2026-05-06T19:02:16Z</updated>
    <published>2000-04-01T00:00:00Z</published>
    <summary type="text">Title: Schistosoma Mansoni and S. Japonicum Cross-Reactive Antigens: Potential Candidate Molecules for a Universal Vaccine
Authors: Abacan, Mary Ann R.; Receno, Pia Angela O.
Abstract: A universal vaccine which protects against both&#xD;
Schistosoma ma11s011i and japonicum infections is not available&#xD;
although it is highly desirable. This study addresses the need&#xD;
to identify cross-reactive antigens between the two schistosome&#xD;
species. This is the first step towards identification of cross reactive&#xD;
antigens which may potentially contribute to a&#xD;
universal schistosome vaccine in the future.&#xD;
In this study, the cross reactivity of S. mansoni antigens&#xD;
with S. japonicum infection sera were tested using the enzyme&#xD;
linked immunosorbent assay. Four S. manosni antigens,&#xD;
namely PB 1, PB2, P28 and P30 were tested with S. japonicum&#xD;
mouse, rabbit and human infection sera. Based on the graph&#xD;
and the statistical analysis using a student t-test, PB2 and P30&#xD;
elicited a positive cross reaction. Between the two, PB2&#xD;
exhibited greater cross reactivity. This data suggests that the&#xD;
S. mansoni antigens PB2 and P30 may be potential universal&#xD;
vaccine candidates.&#xD;
Future work should focus on determining whether S.&#xD;
mansoni antigen PB2 and P30 can protect mice against&#xD;
challenge infection with S. japonicum cercariae.</summary>
    <dc:date>2000-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Partial Purification and Characterization of Phenoloxidase in Coconut Beetle Larvae (Oryctes rhinoceros L.)</title>
    <link rel="alternate" href="http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3591" />
    <author>
      <name>Umali, Janice</name>
    </author>
    <author>
      <name>Yao, Jocelyn</name>
    </author>
    <id>http://dspace.cas.upm.edu.ph:8080/xmlui/handle/123456789/3591</id>
    <updated>2026-03-16T19:02:02Z</updated>
    <published>2002-03-01T00:00:00Z</published>
    <summary type="text">Title: Partial Purification and Characterization of Phenoloxidase in Coconut Beetle Larvae (Oryctes rhinoceros L.)
Authors: Umali, Janice; Yao, Jocelyn
Abstract: Coconut beetle larvae have a protein called&#xD;
phenoloxidase present in their hemolymph that is&#xD;
essential in arthropod immune response. Prior to&#xD;
characterization and isolation of an enzyme designing&#xD;
optimum assay conditions is crucial. This will stabilize&#xD;
the enzyme and ensure optimal activity. In this study,&#xD;
phenoloxidase activity was measured as a function of&#xD;
varying substrates, activators with their incubation&#xD;
periods and incubation temperatures, and buffer pH. The&#xD;
substrate 4-methylcatechol appeared as the best substrate&#xD;
for the enzyme. Among the activators tested, trypsin&#xD;
efficiently activated phenoloxidase within 20-60 minutes&#xD;
incubation periods at 30°C in sodium phosphate buffer&#xD;
with pH ranging from 6.0 to 8.0. The hemolymph was&#xD;
partially purified for pro-phenoloxidase through DEAE&#xD;
and SP ion-exchange chromatography. Fractions positive&#xD;
for enzyme activity were loaded on SOS-PAGE. Partially&#xD;
purified prophenoloxidase shows a molecular weight of&#xD;
85-92 kDa while its active form (phenoloxidase) has a&#xD;
molecular weight of 62-67 kDa.</summary>
    <dc:date>2002-03-01T00:00:00Z</dc:date>
  </entry>
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