An Appreciation; Subject Index; Index of Authors; Index or Organisms

48 Pages·2000·0.75 MB·English

606
K.M, RUDALL: AN APPRECIATION
K,D. Parker
Astbury Departmento f Biophysics, University of Leeds, England
Kenneth MaClaurin Rudall haS been the leading figure in reSearCh intO
all aspects of chitin structure for the past thirty years, but his interests
during a lifetime dedicated to scientific discovery have been much broader .
His fields oi' active research include animal covering and external secretions,
and even that work conceals an extraordinary range of expert knowledge and
an even vaster purview of peripheral awareness in the general field of
molecular biology.
His career has been almost entirely spent at. Leeds University, a
vital center of molecular biological research largely inspired by the long-
time presence there of W. T. Astbury and several distinguished colleagues, of
whom Rudall soon became one, In its early days, that embryonic subject
developed rapidly, thanks to the mutual stimulation of these researchers,
who combinedt he classical methodso f physics and biology with the single
important innovation of x-ray diffraction to form their research techniques.
Rudall was born in New Zealand of an English father and a Scottish
mother his uncle, the mathematicianM acla urin, was president of M.I .T. from
1909 to 1920!. He took a degree in 1932 in physics and zoology and then an
M.Sc. in zoology at the University of Auckland, where he had his "first
conscious contact with chitin, in the canine-type teeth of a carnivorous
worm-eating snail, It was dramatic to stew the massive odontophore in
dilute alkali, when all disappeared except the radula membranew ith its
thousands of teeth," Before leaving New Zealand he wrote two papers for the
Massey Agricultural College on problems connected wi th the growth of
sheep's wool.
Positions in science, then as now, were in short supply so he
moved to England to take a Clothworkers CompanyF ellowship, Thus the
connection with Astbury in 1934 owed something to chance and, as it appeared
at the time, something to ill-fortune. At Leeds his research for the Ph.D,
centered on "X-Ray and Related Studies on the Form and Constitution of
the Biological Cells in Wool and Other Keratin Structures" (cid:1)936!. His
next important paper on the "Physical and Chemical Properties of the Insect
Cuticle" (cid:1)940!, was the result of a fruitful collaboration with G.
Fraenkel of the Department of Zoology at Imperial College, London. The
subjects they discussed there remained among his major interests.
While continuing this collaboration, Rudall was also developing
a~other fielri, which came to rank close to chitin among his major achieve-
ments; this was the study of the mammalian epidermis. Through his original
epidermal preparations, and eventually his isolation of the protein which
he named epidermin, he was able to add a great deal to our understanding
of the structural changeso n extension and contraction of the k-e-m-f group
of proteins, a topic we now relate to helix-random coil-pleated sheet
transformation. Rudall's contribution was to prove the existence of a
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cross-8 structure-- a considerable advanceo ver prevailing ideas. This discovery
was then thought to be of great potential significance for our understanding of
muscle contraction, although that hypothesis has since had to be discarded.
Several years later, while following another line of inquiry, Rudall
more or less accidentally discovered nature 's own r.ross- s struct.ure occurri ng
in the egg stalk of the lacewingf 'ly, Chrysopa. Althought his finding played
only a small part in the growth af modern ideas about, protein structure, it
was significant in confirming beyond doubt tne exist. ence of the cross-6
structu re the earlier diffraction patterns had tended to convince only a
few experts!, andw ast he first clear demonstrationo f protein chain folding,
prOposede ven before these general ideas were widely applied to synthetic
polymer structures. Nawa mply confirmed and publicized by the structure
determinatian of crystalline enzymes,t he cross-6 structu re and the protein
fold the third most commonp rotein confornation! were first set down in
Rudall's work on Chrysopa.
Onea f Rudall's greatest assets was his unusvai ability to master
new techniques and estimate both their potentia'1 scope and their practical
application to his own problems. In 1943 Astbury acqui red one of the t'i rst
four R .C.A . electron microscopesp rovided to Britain under the Lend-Lease
arrangementf rom the United States, Rudall was saon assisting R. Reed in applying
th i s new techni que. Results were obtained, but becauseo f competition for the
use of the new instrument and becauset he techniques then in use were not yet
capable of providing reliable data for chitin, keratin and epidermis, he did
not at that time utilize electrOn microscopy extensively . It remained a
tool well suited to his peculiar kind of experimental ability, however, and
eventually it becameo ne of his principle skills and the main subject of his
teaching at the university .
A little later, infra-red spectroscopy appeareda s a useful tool for
structure analysis, and Rudall, in collaboration with S. E, Darmon, soon
produced two papers of major importance by applying that new technique ta
studies of the a-8 transformation as exemplified by epidermin, the protein
over which he had so muchs tructural control! and to the composition and
structure of a-chitin and chitosan. Just as Astbury failed ta discover the
structures that he had brought to the world 's attention, so RudaI I also
failed narrowly to describe the molecular structure of a-chitin. All the
necessary information was present in his collaboration with garmon, but
the honor passed to D, Carlstram in 1957.
The late 1960s found Rudall surveying tissues, membranesa nd fibers
from a wide range of animal sources and applying x-ray diffraction,
infra-red and electron microscopy to classify them in the light of the
newly discovered structures. general themes link these studies on materials
which, at first sight, seemq uite randomly selected. Onew as Rudall's
interest in tanning and hardening mechanismsg, enerated by his earlier work
with Fraenkel on the insect cu .icle, This led him to examine the collateral
glands and their products in many insects. Fascinating discoveries were made,
and important work was published on the ootheca of mantids and cockroaches,
the eggc aseso f Aspidomarphaan, d the cocoonso f Hydrophilus,a long with
the work on the egg stalks of Chrysopaa lready mentioned, These findings led
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him to make generalizations on 'silks,' which he now regarded as being external
secretions of insects not necessarily closely related to the commonly known
silk f om H~omoh ri. He wrote in 1962 of esi'tks hich e
collagen, silks which are chitin." The importance of this work lay partly in
the wide range of structures found which was thought to owe less to evolutionary
pressures operating on extracellular materials than to intracellular bio-
molecules. This work brought him into collaboratfon with J, 0, Warwicker,
F. Lucas and 0. T. B. Shaw, all of the Shirley Institute.
Rudall also surveyed the occurrence of ~- and 8-chitin in the animal
kingdom in pursuit of a theory that there might be a relation between the
use of collagen by some animals and of the chi tins by others . Whatever
the outcome of the hypothesis, the classificat~on which he arrived at built
a solid foundation for understanding the relation between the HHa nd 8 forms
of chitin originally proposed by Lotmar and Picken in 1950, To these
Rudal 1 added a third form, i, whi ch still awaits general recogni tion, The
most important of these findings was the B-chitin in the pogonophore tubes,
a finding made still more significant by the later discovery of the
remarkable p-chitin spines on diatoms made by Stacey and his co-workers.
These two materials allowed structural determinations by Blac kwell and by
DweltZ! a muCh greater degree Of preCiSiOn than had hithertO been pOSSible.
In the early 1960s, Rudall returned to his interest in wool growth
and the hair follicle, an interest renewed by contact with a fellow
New Zealander, Dry. This reversal of interests was not so far afield as
appears at first glance when one remembers that the general problems of
keratinization aid the hardening of cuticle may not be dissimilar. In the
remaining years before retirement from his university post he was again
working on the protein/chitin complex, gaining a deepev and deeper
understanding of the relation between protein and chitin, obtaining fresh
fnformation from x-ray diffraction, and at last being able to relate the
larger details of structure to visible effects seen in the vastly improved
electron microscope pictures that were by then possible. He was beginning
to form new ideas of the synthesizing and hardening enzymes linked to chitin
rods when he retired from active research in 1975.
ffis published work represents a distinguished record, although, con-
sidering the amount and quality of his research, it fs not voluminous; of a
quiet and reserved disposttion and without ambit ion he was never one to rush
into print. Nor was he enthusiastic about large conferences, although he
was persuaded to attend a fair number. His most important contributions
especially later on! tended to appear in review articles, into which he was
in the habit of inserting his latest results and ideas. As a working
scientist his style will always be remembered by those who know him: a
slightly built man, seemingly tireless in the long hour s spent each day at the
bench or studying the literature, he showed no outward sign of the
scientific long-distance runner he was.
Rudall preferred to do his own experimental work whenever possible.
ffe had a penchant for the "string and sealing wax" tradi ti on, and, as a
result, many of his contri vances had their decidedly humorous aspect; but,
609
he possessedt he scientist's equivalent of the gardener's green thumb, and his
specimenp reparations, often using ingenious and elaborate procedures, were
invariably exactly right for their purpose. What visitors remembear re his
living colonies of exotic insects, mantids, aspidomorpha,s awflies, lacewings
and others, manyo f them maintained in the laboratory for years when research
required it. He hada n uncannya bility to provide just the right conditions
to maintain a healthy stock. Whenh is interst turned to wool growth, he
kept his sheep on a nearby university green, and was apt to be found with a
colony of bees loose in his car or a sheep occupying its back seat.
His attitude to students was a litt'le ambvi alent . Kindly by nature,
he was willing to recognize their existence, but he did not we'Icome under-
graduate teaching and did not go out of his way to attract research students.
His interest always lay in the next problem, and he wasi mpatient of the
unproductivep eri'odt hat precededa student's becomingh elpful.and
independent. Although wary of cormitting his own research to untried hands,
he was extremely helpful and generous in giving time, ideas, and advice
to any who cared to ask. His criticism was always useful, and problems
of any kind, even outside his own wide ranqe of expertise, would always
elicit his interest and valuable conmients. When,i n the 1960s, a number
of postgraduate students camet o him, he accepted that responsibility, and
many were the fortunate beneficiaries of his supervision; a number of
them have since had notable research careers. Wide'Iy knowna s a supreme
experimentalist, to those students he was also known as an "idea man."
In 1952 he was appointed Reader in Professor Astbury's Department
of Biomolecular Structure, an ideal position for him, giving him, as it
did, completef reedomfo r his researcha nd few administrative responsibilities .
After Astbury 's death, Rudall assumedg reater responsibility, and he even
surprised many people by his effectiveness as head of a section in the
new Astbury Departmento f Biophysics at Leeds. Administration and committee
work did not suit his style, however, which still maintained a colonial's
"irreverent disapprovalo f all formalisma nd stiffness." After a few years
he withdrew from this position and retreated to his research.
Rudall's dedication to research is complete, but he also possesses
a dry senseo f humoar nd an independenmt ind, and is readya lwayst o
discuss any topic of the day, serious or trivial. "When science interferes
with private life, then something is wrong," he once said to an astonished
young research assistant. His private life never seemed to interfere wtth
research, either, however; for his pastimes, he gardeneda nd kept bees.
The garden immediately supplied specimenso f sawflies, lacewings, food for
insects, and weeds, when needed, and the bees made a silk with a
remarkably good and different! o-protein pattern as we11a s honey.
Colleagues benefited from both. Whenh e took holidays or traveled to
conferences or to revisit his bi rthp1ace, insects and fibers returned in his
luggage,
Rudall has retired to an estate with a large garden and outbuildings
where, it is rumoured, research still goes on. For any young scientist
looking for a problem to try his hand at a visit would be well worth his
whi 1 e.
610
SELECTEDB IBLIOGRAPHY
1. Thep roteins of the mammaliaenp idermis. In: Advanceisn Protein Chemistry,
vol. 8. (cid:1)952!.
2. With S.E. Darmon!, Infra-red and x-ray studies of chitin. Discussions of
the Faraday Society, no. 9 (cid:1)950!, on Spectroscopesa nd Molecular Structure.
3. The distribution of collagen and chitin, In: The Fibrous Proteins.
Society for Experimental Biology Symposium9 (cid:1)955!.
4. The chitin protein complexo f insect cuticle. Advancesi n Insect
Physiology 1:257 (cid:1)963!.
5. Silk ando ther cocoonp roteins. Tn: ComparativBe iochemistry,H arbon
and Mason eds.!, vol, 4 (cid:1)962!.
6. With F. Lucas!. Extracellular fibrous proteins in silks, In: Comparative
Biochemistry, Harken and Mason eds.!, vol. 268, pp. 475-558.
7. Intracellular fibrous proteins and keratins. In: ComparativBe iochemistry,
Harken and Mason eds.!, vol. 26B. pp, 559-591.
8. With W. Kenchington!. Thec hitin system. Biological Reviews4 8:597(cid:1)9 73!.
611
Sub ect Index
Absidia, 527
Acetate rayon, 131, 1 32
Acetic acid, 103, 104, 171, 172, 174, 199, 556
Aceto~e, 173
2-Acetylamine-d-glucose, 170
N-Acetylaminosugar, 554, 555
Acetylation, of chitin, 406-413
Acetylation, of chitosan, 406-413, 421-425 ' 427-429
Acetylation. see also 9eacetylation
N-acetylg'lucosamine polymers, 6
Acetyl value, of marine chitin, 184, 187-188
Adhesives, and cost of chitin, 64
Adhesive, chitin for use as, 430-435
Adipic acid, 172
Adsorption, 278
of enzymes, 364-365
of metals by chitosan, 444-446, 448
Adsorption chromatography, 341-342
Affinity chromatography, 341-342
Alanine, 256
Alaskan pink shrimp, 183, 186, 188, 190
Algae, 71, 72
Alkaline purification, 22-25
Aluminum nitrate, 173
Amberlite XE-318 resin, 263, 267, 268, 269, 270, 271, 272,
275, 276, 318, 336
American Fish Culture, 255
2-amino-2-deoxy-d-glucose, 210
Animal feed, and chitin-chitosan sales, 86
chitosan in, 224-225
production of, fly larvae for, 70-71
research concerning, 81
use of chitin and chitosan as, 182, 327-332
Animal feed additives, and shell waste, 69
Anion-exchange chromatography, 338-340
Annelids, chitin in, 8
Antarctic convergence, 67
Antarctic krill, 54-62
Antarctic krill, harvesting of, 67-68, 74
Anthozoa, 5
Antibiotics, conxnercial production of, 71
Apolysis, 472
Aquaculture, and production of chitin, 67
Arachnids, 7, 493-496
Arginine, 256
Arthropods, 5, 8, 108
Ascomycetes, chitin in, 14
Ash, in marine chitins, 184, 188, 189
612
~Sub'e ct Index
Aspartic acid, 256
Astacene, 256, 257, 262
Astaxanthin, 254-259, 262
Astaxanthin ester, 254, 255, 256, 257
Baader Fish Bone Separator, 254
Basidiomycetes, 14, 454
Beetle, chitin in, 124
Benzoic acid, 104
Biogeochemical cycle of metals, 289, 294
Biomass, in semi-polluted waters, 8
Bio-Rad Laboratories, 263
Birds, chitinase in digestive tract of, 545
Bivalve, see clams; oysters; mollusca
Blowfly, body composit i on of, 70
Blue crab, 82, 183, 186, 188, 190, 509-514, 516
"Bound" chitin, 23, 25
Brachiopods, 8
Brewery sludge, treatment wit,h chitosan, 220-221, 222,
223, 230
Brown shri mp, 183, 186, 188, 190
Bryozoans, 8
Buchner funnel filtration test, 90
n-Butanol, as TLC developing solvent
Cadmiumw astes, 278, 279, 283, 284
Calcium, in shell waste, 69, 253
Calcium carbonate, in insects, 70
Calcium chloride, as by-product of chitin/chitosan
production, 84
Calcium nitrate, 173
Canthaxanthin, 257, 258, 259, 262
Carboxymethyl ce'Ilulose, solubility of, 170
e-Carotene, 262
Carotenoids, 255-260
Catrix, 296, 297
Catrix-S, 296
Cattle, chitin as nutrient for, 182
Cellulin granules, 11, 14
Cellulose, in cellulin granules, 11
and chit. in chain, ill, 115, 118
co-existing with chitin in cell walls of fungi, 14-15
solubility of, 170
tensile properties of, 131
Cellulose ethers, viscosity of, 174
Centrifugation, coagulant application in, 235-238,
247-248
613
~Sube ct Index
Centrifugation, for dewatering operations, 231, 232
Centrifugation, of food-processing wastes, 2'19
Cephalopods, chitin in, 7
Cestoda, chitin in, 7
Cheese whey, 90
Cheesew hey, treatment with chitosan, 222, 223, 224
Chelation, and chitosan research, 81
Chelation, and Kytex H chitosan, 263-272
Chelation, and transport of metals, 288-292
Chelation, chromatography, 340-341, 344-345
Chelex1 00r esin, 263, 267, 268, 269, 270, 271, 272,
275, 276, 336
Chesapeake Bay blue crab, 82
Chicken, chitinase in gastric Juices and chymeo f,
550-553
Chile, and red crab, 68
a-Chitin and 6-Chi tirl, 517-523
o-Chitin, deformation and transformation in, 131, 133
force-extension curve for, 140
stress-relaxation curve for, 140
structure of, 108-114, 115, 119, 120
sulfate crystals from, 432
tensile properties of, 126-127, 128-129, 131
B-Chitin, acid induced stress-relaxation curve for, 143
and ~-chitin, 517-523
deformation and transformation in, 131, 133-135
force extension curve for, 141
hydrochloric acid/water nysteresis curve for, 142
stress-relaxation curve for, 141
structure of, 108-112, 114-115, 121-123
sulfate crystals from, 432
tensile properties of, 126, 127, 128-129, 131
Chitin, deformation and transformati on in, 1 31, 1 35-136
Chitin, tensile properties of, 126-127, 128-131
Chitin analysis, 22-25, 26-28
Chitinase, 14
cell walls of fungi, 12
extracting from chicken, 550-553
fluorescent-enzyme test, 24
in microorganisms, 587-597
molting cuticle, 472-477
production of, research on, 81
specificity of, 6
assay, 473-474
Chitin biosynthepis, 450-455, 458
Chitin biosynthesis, distribution of, 6
in vitro. 464-469, 471
and polyoxims, 12
Chitin decomposingb acteria, in the sea, 582-584
614
~Sube ct Index
in the soil, 578-579
Chitin digestion, in fish, 554, 560
Chitin distribution, studies of, 5-6
Chitin localization, 5-6
Chitin microfibrils, 450-455, 459, 463
Chitin occurrence, 5-6
Chitin oligomers, 375- 380
Chitinolytic enzymes, 542-547, 554
Chitinolytic microorganisms, 570-575
Chitin synthetase, and cell wall construction, 19
Chitobiase, 14, 475, 543
Chitosan, acetylation of, 406, 413, 421-425, 427-429
hl-acetylation of, 423, 424
0-acetylation of N-acyl chitosans, 424, 429
acid soluble, 14
in animal feed, 224-225, 327-332
in cell walls of zygomycetes, 16
chelating properties of, 263, 272
chi tosanaceous fungi, 72-74
chi tosan-metal complexes, 386-393, 394-405
chromatography, 335-345
composition of, 'l69-171
cross linked, 277-287
cross linked, and laundering shrinkage control, 206-313
decrease in viscosity, 216
effect of pH and salt addition on solution viscosity,
174, 180
enzymatic hydrolysis of, 525-530
equilibrium moisture content as a function of relative
humidity, 174-175, 181
as family of polymers, 170
film-forming capability of, 199-207
as a flocculant, 103
Flonac, 233-234
formation of salts, 277
industrial importance of, 1 69-l 70
insolubi lizing enzymes with, 364-373
Kytex H, 263-272, 274-276
mass spectrum of, 409-413, 418-420
metal binding capacity of, 267, 268-271
molecular weight distribution of, 89-95, 99, 101, 219
net positive charge of, 219
organic acid solvent systems for, 103-106
reaction with glutaraldehyde, 280
removal of metallic ions, 277-287
relationships between viscosity and deacetylation, 244
salt tolerance of, 173
solubility of, 171-172, 245
615
~Sube ct Index
solvent compatibility of, 172- 173
squilla as source of, 210-214
stability of samples, 91
tensile properties of, 128, 130, 131, 132, 139
thermoreversib le chi tosan gels, 193-196, 198
titration of, 280
treatment of food-processing wastes with, 218-226,
228-230
ultrastructure of, 483-485, 487-491
viscosity as a function of concentration, 174, 178
viscosity as a function of temperature, 174, 179
viscosity stability of solutions, 175
and wound-healing acceleration, 296-304
X-ray diffraction patterns from, 208, 209
in Zygomycetes, 12
AMSA-Chitosan3, 38, 339, 340, 350
Diaz-Chitosan, 338, 339, 340, 349
EPIC-Chitosan, 338, 339, 340, 350
0-Hydroxyethyl Chitosan, 338
TU-GLA-Chti osan, 337, 339
U-GLA-Chitosan, 337, 339
U-GLY-Chitosan, 338, 339, 340, 348
Chitosan acetate properties of, 128, 130, 132
Chitosanase, 12, 81, 530
Chitosan color test, 23-24
Chitosan formate, properties of, 128, 130, 132
Chitosan hydrochloride, 407-413, 417
Chitosanolytic microorganisms, 570-575
Chitosan Xanthate, properties of, 128, 130, 132
Chitosomes, 452-455, 460, 462
Chloroethanoi, 182
Chondrophoridae, chitin in, 7
Chromatography, 335-337
absorption, 341-342
affinity, 341-342
anion-exchange, 338-340
che'!ation, 340- 341, 344-345
chitosan, 337
chitosan derivatives, 337-338
high-pressure liquid, 89, 91, 95
ligand exchange, 341
marketing strategy for marine polymers, 64
thin-layer, 342-3 44, 345, 355-356, 358-363
Chrome waste, 279, 285-286
Chromic nitrate, 173
ChytridionIycetes, 14, 15, 454
Ciliates, chitin in, 6
Citric acid, 71, 103, 104, 172