Antarktis-bibliografi er en database over den norske Antarktis-litteraturen.

Hensikten med bibliografien er å synliggjøre norsk antarktisforskning og annen virksomhet/historie i det ekstreme sør. Bibliografien er ikke komplett, spesielt ikke for nyere forskning, men den blir oppdatert.

Norsk er her definert som minst én norsk forfatter, publikasjonssted Norge eller publikasjon som har utspring i norsk forskningsprosjekt.

Antarktis er her definert som alt sør for 60 grader. I tillegg har vi tatt med Bouvetøya.

Det er ingen avgrensing på språk (men det meste av innholdet er på norsk eller engelsk). Eldre norske antarktispublikasjoner (den eldste er fra 1894) er dominert av kvalfangst og ekspedisjoner. I nyere tid er det den internasjonale polarforskninga som dominerer. Bibliografien er tverrfaglig; den dekker både naturvitenskapene, politikk, historie osv. Skjønnlitteratur er også inkludert, men ikke avisartikler eller upublisert materiale.

Til høyre finner du en «HELP-knapp» for informasjon om søkemulighetene i databasen. Mange referanser har lett synlige lenker til fulltekstversjon av det aktuelle dokumentet. For de fleste tidsskriftartiklene er det også lagt inn sammendrag.

Bibliografien er produsert ved Norsk Polarinstitutts bibliotek.

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Bouvetøya

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Abstracts

Engelskjøn, T., & Jørgensen, P. M. (1986). Phytogeographical relations of the cryptogamic flora of Bouvetøya. In Botany of Bouvetøya, south atlantic Ocean. I. Cryptogamic taxonomy and phytogeography (Vol. 185, pp. 71–79). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173542

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Haftorn, S. (1986). A quantitative analysis of the behaviour of the Chinstrap penguin Pygoscelis antarctica and Macaroni penguin Eudyptes chrysolophus on Bouvetoya during the late incubation and early nestling periods. Polar Research, 4(1), 33–45. https://doi.org/10.3402/polar.v4i1.6917

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Jørgensen, P. M. (1986). Macrolichens of Bouvetøya. In Botany of Bouvetøya, south atlantic Ocean. I. Cryptogamic taxonomy and phytogeography (Vol. 185, pp. 23–34). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173542

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Klaveness, D., & Rueness, J. (1986). The supralittoral, freshwater and terrestrial algal vegetation of Bouvetøya. In Botany of Bouvetøya, south atlantic Ocean. I. Cryptogamic taxonomy and phytogeography (Vol. 185, pp. 65–69). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173542

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Mehlum, F. (1986). Fugler i de norske deler av Antarktis. Vår fuglefauna, 9(3), 137–144.
Osnes, K. K., Ellingsen, T. E., & Mohr, V. (1986). Hydrolysis of proteins by peptide hydrolases of Antarctic krill, Euphausia superba. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 83(4), 801–805. https://doi.org/10.1016/0305-0491(86)90150-1

1. The hydrolysis of casein by peptide hydrolases of Antarctic krill, E. superba, has been 2. The peptide hydrolases studied included trypsin-like enzymes, carboxypeptidase A-type of enzymes, carboxypeptidase B-type of enzymes, and an aminopeptidase isolated from Antarctic krill. 3. The trypsin-like enzymes seemed to play a decisive role in the degradation of casein, whereas the carboxypeptidase A, carboxypeptidase B and the aminopeptidase had limited effect when acting on casein alone. When combined with the trypsin-like enzymes, the exopeptidases effected enhanced release of amino acids from the protein. 4. Based on the pattern of amino acids relased from casein by a crude extract of krill, and by the isolated peptide hydrolases either alone or in combination, it is concluded that the purified peptide hydrolases examined comprise the major enzymes responsible for the autoproteolytic activity of krill at neutral- to weakly alkaline pH.

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Osnes, K. K., & Mohr, V. (1986). On the purification and characterization of exopeptidases from Antarctic krill, Euphausia superba. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 83(2), 445–458. https://doi.org/10.1016/0305-0491(86)90394-9

1. Two carboxypeptidase-A type of enzymes and two carboxypeptidase-B type of enzymes effecting hydrolysis of Hipp-l-Phe and Hipp-l-Arg respectively, have been purified from E. superba using gel filtration, affinity chromatography and FPLC-anion exchange chromatography. In addition an aminopeptidase has been partly purified. 2. The carboxypeptidases had mol. wts of 27,000 (carboxypeptidase A) and 31,000 (carboxypeptidase B). 3. Carboxypeptidase A exhibited a broad pH optimum with a maximum at pH 5.5–6.5, whereas carboxypeptidase B had a more narrow pH-optimum with a maximum at pH 7. The aminopeptidase had an optimum at about pH 8.7. 4. The carboxypeptidases were inhibited by the chelating agent 1,10-phenanthroline.

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Øvstedal, D. O. (1986). Crustose lichens of Bouvetøya. In Botany of Bouvetøya, south atlantic Ocean. I. Cryptogamic taxonomy and phytogeography (Vol. 185, pp. 35–56). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173542

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Øvstedal, D. O., & Hawksworth, D. L. (1986). Lichencolous ascomycetes from Bouvetøya. In Botany of Bouvetøya, south atlantic Ocean. I. Cryptogamic taxonomy and phytogeography (Vol. 185, pp. 57–60). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173542

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Schumacher, T. (1986). Lamprospora miniatopsis Spooner, a bryophilous discomycete from Bouvetøya. In Botany of Bouvetøya, south atlantic Ocean. I. Cryptogamic taxonomy and phytogeography (Vol. 185, pp. 61–64). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173542

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Sømme, L. (1986). Terrestrial arthropods of Bouvetøya. Polar Research, 4(2), 231–233. https://doi.org/10.3402/polar.v4i2.6935

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Oversikt over naturområder og forekomster i Norge og polarområdene som er fredet eller vernet pr. 1. januar 1985. (1985). Miljødepartementet.
Suksess i syd: utvidet forskning i Antarktis. (1985). Forsvarets forum, 6(8), 1–3. https://urn.nb.no/URN:NBN:no-nb_digitidsskrift_2016100681033_001

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Eiken, T., & Svendsen, K. (1985). Geodetic-topographic measurements in Dronning Maud Land and on Bouvetøya. In Report of the Norwegian Antarctic research expedition (NARE) 1984/85 (Vol. 22, pp. 19–26). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173240

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Moberg, J. (1985). På ekspedisjon til Sørpolen. Norsk barneblad, 98(3), 50–52. https://urn.nb.no/URN:NBN:no-nb_digitidsskrift_2015071581236_001

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Ohta, Y., & Tørudbakken, B. (1985). Geology of Gjelsvikfjella and western Mühlig-Hofmannfjella. In Report of the Norwegian Antarctic research expedition (NARE) 1984/85 (Vol. 22, pp. 35–41). Norsk Polarinstitutt. https://brage.npolar.no/npolar-xmlui/handle/11250/173240

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Osnes, K. K., & Mohr, V. (1985). On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia Superba. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 82(4), 607–619. https://doi.org/10.1016/0305-0491(85)90497-3

1. Three enzymes effecting hydrolysis of TAME have been purified from E. superba using gel filtration, affinity chromatography and FPLC-anion exchange chromatography. 2. The enzymes had molecular weights of 30,000 (Enzyme I), and 31,000 (Enzymes II and III), respectively, as estimated from SDS-PAGE. 3. pH-optima of about 8.2 were observed for all three enzymes. 4. The enzymes were inhibited by phenyl methyl sulphonyl fluoride (PMSF), tosyl lysyl chloromethyl ketone (TLCK) and soybean trypsin inhibitor (SBTI), whereas tosyl phenyl chloromethyl ketone (TPCK) had no effect on the activity. 5. The enzymes were stable at neutral pH, and only slowly inactivated at highly alkaline pH. Low pH rapidly inactivated all three enzymes. 6. Enzyme I liberated amino acids from casein, whereas Enzymes II and III did not; the latter two being true endopeptidases which effected enhanced amino acid production from casein when mixed with Enzyme I.

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Osnes, K. K., & Mohr, V. (1985). Peptide hydrolases of Antartic krill, Euphausia superba. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 82(4), 599–606. https://doi.org/10.1016/0305-0491(85)90496-1

1. A survey has been made of the peptide hydrolase activities occurring in Antarctic krill, Euphausia superba. 2. A major protein hydrolyzing activity in the pH range of 6–8, and a minor activity at pH 3–4, were detected. 3. Temperature optima of approx. 50°C and 35–40°C, respectively were determined for the neutral and acid peptide hydrolases. 4. Trypsin-like activity, as well as carboxypeptidase A-, carboxypeptidase B-, and aminopeptidase activity were detected in extracts of krill. 5. Considerable variation in total hydrolase activity was observed in different catches of E. superba obtained from the same area. 6. The pattern of release of amino acids during autolytic breakdown of krill proteins was very similar in catches of krill exhibiting considerable differences with respect to total peptide hydrolase activity.

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Sømme, L. (1983). Sommer i Antarktis: blant pingviner, sel og hvalfangstminner. Universitetsforlaget.
Egeland, K. (1982). Norge i polarområdene. Leif Holtedahls forl. https://doi.org/oai:nb.bibsys.no:998421032284702202 URN:NBN:no-nb_digibok_2012052505083

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Last update from database: 3/1/25, 3:17 AM (UTC)