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K J Collier

Publications and source records attributed to K J Collier.

14 recordsLinked to original sources
PubMed2001

Forecasting rehabilitation outcomes for degraded New Zealand pastoral streams.

To understand the timescales and magnitude of responses that can be expected following catchment and riparian rehabilitation, we forecast changes to selected stream ecosystem attributes following tree planting in a pastoral catchment. All planting scenarios were predicted to lead to decreases in daily maximum water temperature after 15-20 years to levels that would be suitable for sensitive invertebrate species. Cooling and reheating were rapid so that most benefits to water temperature along the mainstem were forecast to accrue from shading all of the stream channel network. All planting scenarios were predicted to increase sediment yields over the status quo over the 25-year timeframe examined, with maximal sediment yield occurring about 15 years after planting due to expected erosion of the streambanks under the developing forest shade. Sediment yield was greatest for full catchment planting over 25 years, although sediment yield would be lowest with this scenario over longer timescales. A macroinvertebrate biotic index was predicted to increase by 25% over 15 years if whole catchment afforestation were implemented, compared to 9% if only the 4th order mainstem were planted with riparian trees. The use of ecological forecasting to predict likely outcomes for a range of scenarios should prove useful for prioritising rehabilitation actions.

Agriculture↗
PubMed1989

The Hippocratic Oath.

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Attitude of Health Personnel↗
PubMed1988

Detection of human leukocyte interferon-alpha A and -alpha 2 genes in genomic DNAs by the use of deoxyoctadecyloligonucleotide probes.

Two deoxyoctadecyloligonucleotides complementary to the sequence spanning a single base substitution between human leukocyte interferon (HuIFN) alpha A and alpha 2 genes were efficiently used as probes to distinguish between HuIFN-alpha A and -alpha 2 genes. At 37 degrees C or 42 degrees C under aqueous conditions (0.9 M NaCl), hybridization between both probes and the alpha A and alpha 2 genes without any mismatch was strong, whereas the hybridization with one base mismatch (alpha A probe-alpha 2 gene and alpha 2 probe-alpha A gene) was very weak or negligible. Because the single base substitution of G in the alpha 2 gene for A in the alpha A gene provides an extra HinfI site in the alpha 2 gene at the center of the sequence hybridizing to the alpha 2 probe, digestion with HinfI restriction endonuclease caused complete loss of the hybridization between the alpha 2 probe and the alpha 2 gene. PvuII digestion provides 298-bp fragments hybridizing to the probes only from the alpha A and alpha 2 genes among the known HuIFN-alpha genes. Thus, with the use of these oligonucleotide probes in combination with PvuII and PvuII-HinfI restriction endonuclease digestion, the existence of the sequences corresponding to both IFN-alpha A and IFN-alpha 2 genes in human genomic DNAs was demonstrated. The results also surprisingly indicate that these genes, formerly considered alleles because of their essential identity (1 base pair difference in the coding sequence), are not likely to be alleles, but represent closely related distinct genes.

DNA Restriction Enzymes↗
PubMed1986

Recombinant human interleukin 1 alpha: purification and biological characterization.

Interleukin 1 (IL 1) is a polypeptide hormone produced by activated macrophages that affects many different cell types involved in immune and inflammatory responses. The cloning and expression of a murine IL 1 cDNA in Escherichia coli encoding a polypeptide precursor of 270 amino acids has been reported, and expression of the carboxy-terminal 156 amino acids of this precursor in E. coli yields biologically active IL 1. By using the murine IL 1 cDNA as a probe, we have isolated its human homolog from cDNA generated to lipopolysaccharide-stimulated human leukocyte mRNA. Nucleotide sequence analysis of this cDNA predicts a protein of analysis of this cDNA predicts a protein of 271 amino acids (termed IL 1 alpha) which shows congruent to 61% homology to its murine counterpart but only 27% homology to a recently characterized human IL 1 precursor (IL 1 beta). We have expressed the carboxy-terminal 154 amino acids of IL 1 alpha in E. coli, purified this protein to homogeneity, and have compared it with pure recombinant murine IL 1 in several different IL 1 assays based on murine and human cells. Recombinant IL 1 is capable of stimulating T cell and fibroblast proliferation and inducing fibroblast collagenase and prostaglandin production, thus proving that a single molecule has many of the activities previously ascribed to only partially purified IL 1 preparations. Our results indicate that there exists a family of at least two human IL 1 genes (alpha and beta) whose dissimilar protein products have similar biological activities.

Amino Acid Sequence↗
PubMed1984

Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes.

An oligonucleotide probe specific for the amino acid sequence at the biotin site in pyruvate carboxylase was used to screen a human liver cDNA library. Nine cDNA clones were isolated and three proved to be pyruvate carboxylase clones based on nucleotide sequencing and Northern blotting. The biotin site amino acid sequence of human pyruvate carboxylase agreed perfectly with that of the sheep enzyme in 14 consecutive positions. The highly conserved amino acid sequence, Ala-Met-Lys-Met, found at the biotin site in most biotin-containing carboxylases was also present in human pyruvate carboxylase. The termination codon was located 35 residues 3' to the lysine residue at which the biotin is attached. Therefore, the biotin cofactor is covalently linked near the carboxyl-terminal end of the carboxylase protein. These data are consistent with that observed for other biotin-containing carboxylases and strongly suggests that the genes encoding the biotin-containing carboxylases may have evolved from a common ancestral gene. Northern blotting of mRNA isolated from human, baboon, and rat liver demonstrated that the pyruvate carboxylase mRNA was 4.2 kilobase pairs in length in all species examined. Southern blot analysis of genomic DNA isolated from human-Chinese hamster somatic cell hybrids localized the pyruvate carboxylase gene on the long arm of human chromosome 11. The human cDNA was also used to quantitate pyruvate carboxylase mRNA levels in a differentiating mouse preadipocyte cell line. These data demonstrated that pyruvate carboxylase mRNA content increased 23-fold in 7 days after the onset of differentiation.

Adipose Tissue↗
PubMed1984

Cloned cDNA to cholecystokinin mRNA predicts an identical preprocholecystokinin in pig brain and gut.

Molecular cloning has established the structure of preprocholecystokinin in porcine cerebral cortex and duodenal mucosa. This precursor is 114 amino acids long, is identical in brain and gut, contains all the cholecystokinin (CCK) peptides previously isolated, and has the characteristics of a prohormone. It contains a putative amino-terminal signal peptide, basic processing sites, and a carboxyl-terminal amidation signal. The CCK mRNAs from brain and gut are approximately 850 nucleotides long and differ by only a few single base changes. This analysis establishes by a strict criterion that CCK is synthesized in both brain and gut and that the different distributions of molecular forms of CCK in the two tissues are most probably a consequence of tissue-specific posttranslational events.

Animals↗
PubMed1984

Cloning and sequence analysis of a cDNA encoding rat preprocholecystokinin.

Poly(A) RNA was isolated from a rat medullary thyroid carcinoma that exhibited high levels of immunoreactive cholecystokinin (CCK). Double-stranded cDNA was synthesized from the poly(A) RNA and inserted into the Pst I site of pBR322. Bacterial colonies containing CCK cDNA were identified using the hybridization probe d(T-C-C-A-T-C-C-A-N-C-C-C-A-T-G-T-A-G-T-C). The sequence of the probe was deduced from the known amino acid sequence of porcine CCK-8, Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2. The nucleotide sequence of the cDNA complementary to the mRNA of rat preprocholecystokinin was determined. The cDNA contains 33 nucleotides in the 5'-noncoding region, 199 nucleotides in the 3'-noncoding region, and 345 nucleotides coding for a precursor to CCK, which is 115 amino acids (Mr, 12,826). Examination of the rat CCK gene revealed a suggested transcriptional control sequence analogous to the "TATA" sequence located 33 nucleotides upstream from a proposed transcriptional start site. The amino acid sequence of CCK-39 is flanked by both amino-terminal and carboxyl-terminal extensions. Analysis of CCK mRNA showed that it is approximately equal to 750 nucleotides long. CCK mRNA of the rat brain and intestine appeared to be identical in size to the CCK mRNA of the carcinoma.

Amino Acid Sequence↗
PubMed1983

Cloning and sequence analysis of cDNA for the precursor of human growth hormone-releasing factor, somatocrinin.

Molecular cloning has established the primary structures of two precursors of the human pancreas growth hormone-releasing factor (hpGRF-44), somatocrinin. Both polypeptides contain the sequence of hpGRF-44 flanked by basic processing sites. Furthermore, the precursors include a putative signal sequence and a carboxyl-terminal amidation signal for hpGRF-44. The two forms of mRNA code for pre-pro-GRF-107 and pre-pro-GRF-108. Pre-pro-GRF-108 differs from pre-pro-GRF-107 by the insertion of a serine in the carboxyl-terminal portion of the precursor. In vitro translation of tumor poly(A)+ RNA followed by immunoprecipitation with GRF-specific antiserum and gel electrophoresis showed the molecular weight of preprosomatocrinin to be approximately 13,000, which is in good agreement with the molecular weight deduced from the sequences of the cDNA clones.

Amino Acid Sequence↗
PubMed1981

Sequence analysis of a cDNA coding for a pancreatic precursor to somatostatin.

A synthetic oligonucleotide having the sequence d(T-T-C-C-A-G-A-A-G-A-A) deduced from the amino acid sequence Phe-Phe-Trp-Lys of somatostatin-14 was used to prime the synthesis of a cDNA from channel catfish (Ictalurus punctatus) pancreatic poly(A)-RNA. The major product of this reaction was a cDNA fragment of 565 nucleotides. Chemical sequence analysis of the cDNA fragment revealed that it was complementary to a mRNA coding for somatostatin. The 565-nucleotide cDNA hybridizes strongly with a poly(A)-RNA estimated to be 1000 nucleotides in length. An amino acid sequence of the somatostatin precursor was predicted from the nucleotide sequence. Oyama et al. [Oyama, H., Bradshaw, R. A., Bates, O. J. & Permutt, A. (1980) J. Biol. Chem. 255, 2251-2254] have reported the isolation of a somatostatin from the catfish that is 22 residues in length (somatostatin-22). This peptide differs from somatostatin-14 in amino acid sequence. The cDNA sequence obtained by this laboratory codes for somatostatin-14 and predicts another somatostatin gene product from this species. Thus it would appear that there are at least two somatostatin gene products.

Animals↗
PubMed1979

The use of barium salts of protected deoxyribonucleoside-3' p-chlorophenyl phosphates for construction of oligonucleotides by the phosphotriester method: high-yield synthesis of dinucleotide blocks.

A new experimental approach to the synthesis of polydeoxyribonucleotides via the phosphotriester method involves construction of oligonucleotide blocks by direct use of the easily prepared barium salts of O5',N-protected deoxyribonucleoside-3' p-chlorophenyl phosphates as the key monomers in condensation reactions. The procedure has been demonstrated by the rapid synthesis in high yield and purity of all sixteen fuly protected dinucleotides (Formula: see text) (where dN' = dT, dbzC, dbzA, or dibG; (Formula: see text) This set of molecules constitutes a "syllabary" for the preparation of defined sequence oligonucleotides.

Barium↗