Hemolymph ice nucleating proteins from the New Zealand alpine weta Hemideina maori (Orthoptera: Stenopelmatidae)

Comparative Biochemistry and Physiology -- Part B: Biochemistry and

Volumn 112, Issue 3, 1995, Pages 535-542

  Wilson, P ^a   Ramlov, H ^b  

^a UNIVERSITY OF OTAGO   (New Zealand)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Dynamic light scattering; Freeze tolerance; Ice nucleating agents; Supercooling point; Weta, Hemolymph, Cold tolerance, Orthoptera

Indexed keywords

ANIMAL TISSUE; ARTICLE; COLD TOLERANCE; FREEZING; HEMOLYMPH; HYDRODYNAMICS; ICE NUCLEATION; INSECT; LIGHT SCATTERING; NONHUMAN; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN STRUCTURE; ULTRAFILTRATION;

ANIMALIA; HEMIDEINA MAORI; INSECTA; ORTHOPTERA; STENOPELMATIDAE;

EID: 0028825411     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/0305-0491(95)00080-1     Document Type: Article

References (21)

1. Antifreeze glycoproteins from an Antarctic fish: Quasi-elastic light scattering studies of the hydrodynamic conformations of antifreeze glycoproteins
2. Surface properties and size of the ice nucleation site in ice nucleation active bacteria: Theoretical considerations
3. Freeze-tolerance adaptations including haemolymph protein and lipoprotein nucleators in the larvae of the cranefly Tipula trivittata
4. Size effect in heterogeneous nucleation
5. Antifreeze activity of Antarctic fish glycoprotein and a synthetic polymer
6. Size of bacterial ice-nucleation sites measured in situ by radiation inactivation analysis
7. Haemolymph composition of two species of New Zealand weta Hemideina (Orthoptera: Stenopelmatidae)
8. Clustering of ice nucleation protein correlates with ice nucleation activity
9. Freezing tolerance of the New Zealand alpine weta Hemideina maori Hutton (Orthoptera: Stenopelmatidae)
10. Artemia cysts at subzero temperatures studied by differential scanning calorimetry
11. Ice formation in the freeze tolerant alpine weta Hemidiena maori Hutton (Orthoptera: Stenoplematidae)
12. Low-temperature conditioning of the ice nucleation active bacterium Erwinia herbicola
13. Purification, composition and physical properties of a thermal hysteresis “antifreeze” protein from larvae of the beetle Tenebrio molitor
14. Heterogeneous ice nucleation by bacteria
15. The physical basis of action of biological ice nucleating agents
16. Hydrodynamic diameter of fish antifreeze molecules by quasi-elastic light scattering
17. Stabilisation of supercooled fluids by thermal hysteresis proteins
18. Nucleating agents in coldhardy insects
19. Ice nucleating agents in coldhardy insects
20. A method for quantitative determination of ice nucleating agents in insect hemolymph