2
have been possible without the support of the captain and crew of Wv Hero and the help of other scientists and personnel at Palmer Station. References Cielecka, D., and K. Zdzitowiecki. 1981. The tapeworm Microsoma- canthus shetlandicus sp. n. (Hymenolepididae) from the dominican gull of king George Island (South Shetlands, Antarctica). Bulletin de l'Academie Polonaise des Sciences, 29, 173-180. Fuhrmann, 0. 1921. Die Cestoden der Deutschen Sudpolar Expedition 1901-1903. Deutsche Sudpolar Expedition 1901-1903 (Drygalski) Zoo- logie, 8, 467-542. Graefe, G. 1968. Paramonostomum antarcticum n. sp. (Trematoda: Notocotyliadae) und Beobachtungen zur Larvenentwicklung in der Antarktis. Zeitschrift far Parasitenkunde, 30, 207-232. Johnston, T. H. 1937, Australian antarctic expedition 1911-1914. Ce- stoda., 10(4), 5-71. Jones, N. V., and I. C. Williams. 1969. The nematode and acanthocephalan parasites of the sheathbill, Chionis alba (Gmelin) at Signy Island, South Orkney Islands and a summary of host parasite relationships in the sheathbill. Journal of Helminthology, 43, 59-67. Prudhoe, S. 1969. B.A.N.Z. Antarctic Research Expedition 1929-1931. Cestodes from fish, birds and whales. 8, 171-193. Properties of antifreeze proteins from fish blood and penguin egg-white proteins DAVID T. OSUGA and ROBERT E. FEENEY Department of Food Science and Technology University of California-Davis Davis, California 95616 YIN YEH Department of Applied Science University of California-Davis Davis, California 95616 Yin Yeh, physicist in the Department of Applied Science at the University of California-Davis (ucD), and Michael Knauf, Master of Science student from UCD, spent approximately 1 month at McMurdo-Station solely to acquire fish blood serum. The two arrived on 1 November and were able to begin opera- lions in a fish house on 10 November 1982. They obtained a total yield of approximately 1 liter of blood serum from 1,250 spec- imens of Pagothenia borchgrevinki. As the blood serum was ob- tained, it was centrifuged from the cellular material and frozen for transport back to UCD. Specimens of Dissostichus mawsoni, which had been used as experimental fish in the aquarium at McMurdo station by A. L. DeVries, were also obtained and bled (with Dr. DeVries' help) yielding approximately I liter of diluted serum, which was frozen and taken to Davis. The crude fractionations have been completed on most of the serum returned from Antarctica. Final purifications of the anti- freeze glycoproteins, however, will take more time. The yields on the P. borchgrevinki serum were comparable to our earlier studies of both antarctic and arctic species, measuring approx- imately 33.8 grams of total antifreeze. The purification of these components will, of course, greatly reduce the overall yields. Unfortunately, the activities found in the D. rnawsoni serum were only about 36 percent of what had been previously ob- tained, undoubtedly due to the biological history of the fish. Nevertheless, the amount of material obtained in the serum was approximately 12 grams, and this will be important for our studies. The usual yields in the antifreeze proteins from P. borchgrevinki for the so-called larger molecular-weight "active" components should be approximately 3.9 grams, and for the smaller molecular-weight much-less-active material, the yield should be approximately 29.9 grams. Correspondingly, the D. mawsoni yield will be approximately 36 percent lower because purifying materials from sera of lower activity is more difficult. Studies have continued on the potentiation of antifreeze ac- tivities in mixtures of small and large glycoproteins when ice made from deeply supercooled solutions is used to nucleate the solutions (Burcham et al. 1982, 1983). Thus, when the smaller peptide chains of antifreeze glycoproteins from P. borchgrevinki are tested with ice made at - 1°C, they function, but when tested with ice made at —6°C, they do not function. However, when the smaller ones are mixed with the larger ones, they function with ice made at —6°C. Both the structure of the ice and the structure of the antifreeze proteins influence this poten- tiation; this might be of significance for understanding how the antifreeze proteins function at ice surfaces. During the past year, we published a long-term study on the sulfhydryl-containing proteins of penguin egg white (Osuga et al. 1983). A "new" major egg-white albumin in penguin egg white was described. We have named this Penalbumin (table). Penalbumin replaces about half of the ovalbumin in the egg white and has some resemblances to the penguin ovalbumin but has twice the content of carbohydrate and no phosphorous. The eggs of the two species of penguins tested—the Adélie (Pygoscelis adeliae) and the emperor (Aptenodytes forsteri)—both contain this interesting protein. This work was supported in part by National Science Founda- tion grants DPP 81-16963 and DPP 78-26015 and National In- stitutes of Health grant GM 23817. References Burcham, T. S., D. T. Osuga, Y. Yeh, and R. E. Feeney. 1982. Anti- freeze glycoprotein activity as a function of ice crystaline habit. Cryo- Letters, 3(3), 173-176. Burcham, T. S., I). T. Osuga, Y. Yeh, and R. E. Feeney. 1983. Supercool- ing and the activity of antifreeze glycoproteins from Eleginus gracilis. Federation Proceedings, Federation of American Societies for Experimental Biology, 42(7), 1998 (Abstract 1409). 208 ANTARCTIC JOURNAL

Properties of antifreeze proteins from fish blood and ... · month at McMurdo-Station solely to acquire fish blood serum. The two arrived on 1 November and were able to begin opera-lions

  • Upload
    others

  • View
    3

  • Download
    0

Embed Size (px)

Citation preview

Page 1: Properties of antifreeze proteins from fish blood and ... · month at McMurdo-Station solely to acquire fish blood serum. The two arrived on 1 November and were able to begin opera-lions

have been possible without the support of the captain and crewof Wv Hero and the help of other scientists and personnel atPalmer Station.

References

Cielecka, D., and K. Zdzitowiecki. 1981. The tapeworm Microsoma-canthus shetlandicus sp. n. (Hymenolepididae) from the dominicangull of king George Island (South Shetlands, Antarctica). Bulletin del'Academie Polonaise des Sciences, 29, 173-180.

Fuhrmann, 0. 1921. Die Cestoden der Deutschen Sudpolar Expedition

1901-1903. Deutsche Sudpolar Expedition 1901-1903 (Drygalski) Zoo-logie, 8, 467-542.

Graefe, G. 1968. Paramonostomum antarcticum n. sp. (Trematoda:Notocotyliadae) und Beobachtungen zur Larvenentwicklung in derAntarktis. Zeitschrift far Parasitenkunde, 30, 207-232.

Johnston, T. H. 1937, Australian antarctic expedition 1911-1914. Ce-stoda., 10(4), 5-71.

Jones, N. V., and I. C. Williams. 1969. The nematode andacanthocephalan parasites of the sheathbill, Chionis alba (Gmelin) atSigny Island, South Orkney Islands and a summary of host parasiterelationships in the sheathbill. Journal of Helminthology, 43, 59-67.

Prudhoe, S. 1969. B.A.N.Z. Antarctic Research Expedition 1929-1931.Cestodes from fish, birds and whales. 8, 171-193.

Properties of antifreeze proteins fromfish blood and penguin egg-white

proteins

DAVID T. OSUGA and ROBERT E. FEENEY

Department of Food Science and TechnologyUniversity of California-Davis

Davis, California 95616

YIN YEH

Department of Applied ScienceUniversity of California-Davis

Davis, California 95616

Yin Yeh, physicist in the Department of Applied Science atthe University of California-Davis (ucD), and Michael Knauf,Master of Science student from UCD, spent approximately 1month at McMurdo-Station solely to acquire fish blood serum.The two arrived on 1 November and were able to begin opera-lions in a fish house on 10 November 1982. They obtained a totalyield of approximately 1 liter of blood serum from 1,250 spec-imens of Pagothenia borchgrevinki. As the blood serum was ob-tained, it was centrifuged from the cellular material and frozenfor transport back to UCD. Specimens of Dissostichus mawsoni,which had been used as experimental fish in the aquarium atMcMurdo station by A. L. DeVries, were also obtained and bled(with Dr. DeVries' help) yielding approximately I liter of dilutedserum, which was frozen and taken to Davis.

The crude fractionations have been completed on most of theserum returned from Antarctica. Final purifications of the anti-freeze glycoproteins, however, will take more time. The yieldson the P. borchgrevinki serum were comparable to our earlierstudies of both antarctic and arctic species, measuring approx-imately 33.8 grams of total antifreeze. The purification of thesecomponents will, of course, greatly reduce the overall yields.Unfortunately, the activities found in the D. rnawsoni serumwere only about 36 percent of what had been previously ob-tained, undoubtedly due to the biological history of the fish.Nevertheless, the amount of material obtained in the serum was

approximately 12 grams, and this will be important for ourstudies. The usual yields in the antifreeze proteins from P.borchgrevinki for the so-called larger molecular-weight "active"components should be approximately 3.9 grams, and for thesmaller molecular-weight much-less-active material, the yieldshould be approximately 29.9 grams. Correspondingly, the D.mawsoni yield will be approximately 36 percent lower becausepurifying materials from sera of lower activity is more difficult.

Studies have continued on the potentiation of antifreeze ac-tivities in mixtures of small and large glycoproteins when icemade from deeply supercooled solutions is used to nucleate thesolutions (Burcham et al. 1982, 1983). Thus, when the smallerpeptide chains of antifreeze glycoproteins from P. borchgrevinkiare tested with ice made at - 1°C, they function, but whentested with ice made at —6°C, they do not function. However,when the smaller ones are mixed with the larger ones, theyfunction with ice made at —6°C. Both the structure of the iceand the structure of the antifreeze proteins influence this poten-tiation; this might be of significance for understanding how theantifreeze proteins function at ice surfaces.

During the past year, we published a long-term study on thesulfhydryl-containing proteins of penguin egg white (Osuga etal. 1983). A "new" major egg-white albumin in penguin eggwhite was described. We have named this Penalbumin (table).Penalbumin replaces about half of the ovalbumin in the eggwhite and has some resemblances to the penguin ovalbuminbut has twice the content of carbohydrate and no phosphorous.The eggs of the two species of penguins tested—the Adélie(Pygoscelis adeliae) and the emperor (Aptenodytes forsteri)—bothcontain this interesting protein.

This work was supported in part by National Science Founda-tion grants DPP 81-16963 and DPP 78-26015 and National In-stitutes of Health grant GM 23817.

References

Burcham, T. S., D. T. Osuga, Y. Yeh, and R. E. Feeney. 1982. Anti-freeze glycoprotein activity as a function of ice crystaline habit. Cryo-Letters, 3(3), 173-176.

Burcham, T. S., I). T. Osuga, Y. Yeh, and R. E. Feeney. 1983. Supercool-ing and the activity of antifreeze glycoproteins from Eleginus gracilis.Federation Proceedings, Federation of American Societies for ExperimentalBiology, 42(7), 1998 (Abstract 1409).

208 ANTARCTIC JOURNAL

Page 2: Properties of antifreeze proteins from fish blood and ... · month at McMurdo-Station solely to acquire fish blood serum. The two arrived on 1 November and were able to begin opera-lions

Physical and chemical properties of penalbumin, penguin ovalbumin, chicken ovalbumin, penguin serum albumin, and bovine serum albumin

Property Penalbumin Penguin Chicken Penguin Bovineoval buminovalbuminserum albuminserum albumin

Molecular weight

p't

Carbohydrate (%)1%

E280

PhosphorusTotal (S)CSulfhydrylsDisulfide

a From Feeney 1982.b "nd' denotes not determined.

Values from amino acid composition.Amount determined by —SH reagents.

a Values determined by dividing by 2 the difference between the total (S) and the —SH values.

"S20 ," denotes sedimentation coefficient corrected to 20°C and water. "pi" denotes the characteristic pH of the protein. E denotes the optical

absorption of a 10 milligrams per biilliliter solution at 280 nanometers

61,000

48,000

45,000

66,000

66,0003.41

3.25

3.19

4.12

4.404.16

3.98

4.48 ndb nd15

7

3 <0.2

05.68

6.77

7.43

6.84

6.14

0

0,1,2

0

06

6

6

35

352' 3d(4) 4d <1"'

2e 17e

17

Feeney, R. E. 1982. Penguin egg-white and polar fish blood-serumproteins. International Journal of Peptide and Protein Research, 19(3),215-232.

Osuga, D. T., M. Aminlari, C. Y.-K. Ho, R. G. Allison, and R. E.

Feeney. 1983. Sulfhydryl proteins of penguin egg white: Ovalbuminand penalbumin. Comparisons with penguin serum albumin, chick-en ovalbumin, and bovine serum albumin. Journal of Protein Chemistry,2(1), 43-62.

• Breeding and feeding ecologies ofpygoscelid penguins

WAYNE Z. TRIVELPIECE, SUSAN C. TRIVELPIECE,NICHOLAS J. VOLKMAN, and STEPHEN H. WARE

Point Reyes Bird ObservatoryStinson Beach, California 94970

We have completed the final year of a project designed tocompare the breeding and feeding ecologies of the sympatricpopulations of pygoscelid penguins at Point Thomas, KingGeorge Island, South Shetland Islands (62°10'S 58°30'W). Wespent 5 October 1982 to 5 March 1983 at the Polish Academy ofScience's Arctowski Station, where we have been visiting scien-tists throughout the 3-year tenure of this project. Our broadobjectives were to collect detailed quantitative data on thebreeding biology of the three penguin species and to determinethe type and amount of prey they consumed throughout thebreeding season.

During 1982-1983, unlike two previous seasons (1977-1978and 1981-1982), the three pygoscelid penguin species had very

different reproductive success rates. Adélie and chinstrap pen-guins fledged only 0.67 and 0.56 chicks per breeding pair,respectively, significantly below their 1.00 and 1.02 mean chicksfledged during 1977-1978 and 1981-1982. However, gentoopenguins fledged 1.17 chicks per pair in 1982-1983, a successrate higher (but not significantly) than their 1.01 chicks fledgedper pair mean for the earlier period. We believe that differencesin the courtship strategies and incubation routines of the threepygoscelids may have accounted for these results. Adélie andchinstrap penguins fasted for 2-3 weeks between arrival andegg laying. Following clutch completion, the male Adélie as-sumed the first incubation shift and fasted another 10-19 days;the female went to sea to feed. In chinstraps, either the male orfemale took the first incubation shift of approximately 7 days.Unlike its congeners, gentoo penguin pairs feed daily early incourtship and relieve each other at the nest about every 24 hoursthroughout incubation.

The major cause of egg mortality among Adélies andchinstraps was desertion of the nest by the incubating bird priorto the return of its mate. The mean first incubation shift amongAdélie males was 15-17 days in the 1982-1983 season, signifi-cantly longer than the mean 10-12 days shift in 1981-1982. Dueto an apparent food shortage early in the season, neither Adé-lies nor chinstraps could recover from their pre-incubation fastsin time to relieve their mates. Gentoo penguins were able to

1983 REVIEW 209