close

Вход

Забыли?

вход по аккаунту

?

код для вставки
‘
Patented Dec. 31, 1946’ I
I‘
_
2,413,501
,
UNITED. STATES-PATENT OFFICE» "
FIBERS mom GLOBULAB AND
ART1FICIALmasons
rao'rams
,
Oskar Huppert, New York, N. Y.
‘No Drawing. Application February 12,1945,
Serial No. 577,593
serum. (01. 260-119)
contracted. More .or less ‘cross linked by means
This application is a continuation in part of
theone ?led on May 24, 1944, bearing Serial No.
537,190, now U. S. Patent 2,384,421. My inven
tion deals'with ?bers made from proteins. The
object of this'invention is to produce dispersions
of secondary valenc'es through polar groups, salt
linkages they form with their side chains a co
planar three dimensional arrangement. Because
of free rotation around single bonds the struc
tural units of natural ?bers arecapable of being _ '
' ofI proteins, which can be used to make ?bers,
oriented and to form crystal lattices which favors
?ber strength and ?exibility, it there is not comand softness and are valuable as ?bers.
,
pletely cross linking.
A further object resides in processes for mak
The current view of globular protein accord--.
10'
ing these dispersions. Other objects of the in
ing X-ray analysis is that crystalline globular
vention will appear as the description proceeds.
proteins have a compact structure, that the very
These objects are accomplished by the follow
regularly built molecules contain a considerable
ing invention in which dispersions of pseudothio- - ' amount of water. The very highly ordered struc
which have strength, water resistance, ?exibility
hydantoin-protein salts of alkyl-benzeneqsu'l
ionic acid of the general formula as follows:
ture, revealed by .X-ray photographs of protein.
15
crystals, discloses, that the chains of the globular .
proteins must be built into a very systematic
CHr--S\
I
- pattern of folds. On treatment with denaturating '
agents a breakdown of this special ordered struc
'20 ture occurs and ‘the resulting products aggre
gate on coagulation into ?brous bundles which
wherein; protein’-NHz denotes protein, are used , ‘have been shown by'X-ray study to be of the
beta keratin type. An intimate relation between
to produce arti?cial ?bers from globular and
the ?brous and the globular proteins is'there-v
?brous proteins by spinning and stretching,
hardening, pre and after treatment methods with. 25 with indicated. Therefore a transformation of
globular proteins in ?brous proteins should be
various modifyingagents already known to the
possible. However, neither the cyclol hypothesis
art.
_
of D. M. Wrinch (1936) nor the models of Hug
All proteins
gins (1940) have shown wherein the special con
of the chains of the globular proteins
30 ?guration
consists and the X-ray' diffraction \patterns of
I have discov I
the globular proteins arev still not su?iciently
djthat the ‘reaction takes place
rnmonia, where a protein is
also in presenc
e precipitated on the acid
used which {woiil ,
side of its vfisfoelectric point. According to this
advanced.
_
,
Based on the reaction of carbon disul?de_-and
proteins, protein hydrolysates, alpha amino acids,
35
invention ?bers may be prepared either from an
U. S. Patent 2,112,210 and on the physiological ‘
ammonia alkaline-aqueous solution where a
native proteins in the living organism I conceived
protein is used as for instance'casein, soybean
or peanut protein, egg albumin, reduced. chicken
and physical-biochemical reactions of natural,
' in my publication
feather keratin .or vfrom an alcoholic-aqueous 40
solution where a protein is, used as for instance
zein, gliadin or. otherfprqlamines, protamines.
.teins are built up on
from normal proteyls,
The present;i_dea ‘ ' ‘ hf structural units or natu
ral ?bers asst
“Das Protein” Wien, 1933, the
all globular pro
“Proteyl-theory.” Accordingly
the same general pattern
. . . N-—'-_
in
emolecules developed by gist
bury, Mark and’Meyer and others are not able 45
to disclose the structural difie' ence of globular
and ?brous proteins. _My;work to establish the
structure of th rot ins starts from early state
ments, publis‘
.uration der '
'
=5 0H . . .
or from pseudo-proteyls, I
'
‘Konstitution ,und Kon?g
sto?e, Wien-Liepzig, 1928”, so "
and is used in the present application. Textile
?bers should have strength and ?exibility.
Globular (sphero) proteins as such are not‘ ?t
for preparing ?bers, only ?brillar (linear). pro
.
.-. CR=
NH
,
a
a
I
which six of each are in space con?gurated under
an angle of 60 degrees in the boat type, represent
ing‘the isomeres of the elementary units. of the
teins are, capable of forming ?bers which in cer 55 protein. The elementary unit exists in three
tain circumstances are su?iciently ‘tough and
stereoisomeric forms. The normal form showing
elastic to possess some technical interest. These , relations with dioxopiperazines, voxazolines, tri
azines, acetaldehyde, the pseudo form with ,
both classes of natural high polymers are di?er
ent in kind of their structural units. Natural
hexoses, hexosamines, glucose, the purin form
?bers consist of open, long polypeptide chains,
60 with beta ketonic acids, acetone, pyridine, purin
which may be completely extended (beta-keratin
and‘pyrimidine glucosides, purin bases such as
type) or coiled (alpha-keratin type) or super
2,413,501
3
'
,
adenine, guanine and pyrimidine bases. such as
This network of proteyls changes in a bundle .
of polypeptide chains resulting from the conver
sion of the peptide-betain linkage in a peptide
cytosine and uracil, the combined normal-pseudo
form with isoprene, phytol, terpene derivatives
and carotenoides. The following formulas give
linkageas follows:
the structure and con?guration of the elementary
'
I units of the protein:
ISOMERES OF THE ELEMENTARY UNITSOF
10
and thus e?’ecting the transformation of the
globular proteins inthe ?brous proteins.
At last the di?erence of globular and ?brous
proteins consists in the deposition of water (in
ternal hydration) between the proteyls girders of
the individual elementary units. According the
proteyl theory in contrast to Emil Fischer’s con
ception proteins are not built up from amino acids
having the structure, (j—CO-—CH(R)—NH—-)n
but from hydrated proteyls having the structure
20
25
Any non-protcolytic modi?cation of the uniquev
structure of a native protein resulting under the
in?uence of denaturating agents is a step in the
continuous line of a dynamic process leading from
the very systematic. and speci?c 'pattern of the
30
six in space con?gurated p'roteyls under break
down of the proteyl-girder to unfolded poly
peptide chains of the beta keratin type with the
intermediate stages of super contracted and coiled
polypeptide chains.
_
Associating water as well on the polar, hydro
40
philic groups of their side chains (external hy
dration) as, on the oxygen atoms _of the girder,
the hydration degree of the proteins turns out to
be decisive for the osmotic pressure and-viscosi
ties of the protein solutions while the denatura
tion-kinetic of the proteins becomes the deter
-minative' factor for their ability to be spun in
?bers.
‘Solutions containing salts of pseudothio
45 hydantoin-protein (?brous and globular). with
alkyl-benzene sulfonic acids'can be used to .pre
cipitate the synthetic protein in a coagulating
bath into a, plastic state, favorable for drawing
into ?bers. 'On the alkaline side of the isoelectric .
point anions of the alkyl-benzene sulfonic acid
exert an in?uence conducive to the transforma
tion or the globular proteins in ?brous proteins
by drawing the ?bers over 300%.
_
The following examples are illustrative for all
55 proteins and will serve to show certain speci?c
details of the invention, however, it is to, be under?
Two such normal proteyls, belonging .to' two
stood that the speci?c details as set forth in the
different elementary units, would formally result
examples are not to be considered as limitative ‘
by condensation of two mol alpha amino acids in
of the invention.
,
the “zwitter ion form” as follows:
60
‘
_
. in .
NHw
HR
I.‘ """"
00-
E
‘Casein ?bers are spun from a solution having
‘:JBR
.
- the following composition: 110 grams of‘ casein
are'soaked in 555 cc. of water at 24° C. containing
"""
4. . . .
Eirample 1
E
65 9.4 'g. monochloracetic acid, 7.6 g. ammonium
thiocyanate, 8.1 g.'p-toluene sulfonic acid cryst.
and 21 cc. concentrated ammonium hydroxide
é
IHR
:
. . . . NH .
. —— |
{
.
with stirring. After three hours the dispersion is
heated to 45° C. and the ripened and deaerated
70 solution- is forced through a spinneret of forty
holes and of a diameter of 0.004 inch into a co
agulating bath having the composition: water 100
cc., conc. sulfuric acid 15 g., anhydrous sodium
showing the peptide-betain linkage encircled.
sulfate 20 g., aluminum sulfate (hydrate) 10 g. ,
75 The coagulated ?bers are afterwards stretched in
2,418,501
lution. The fibers are washed with cold water
a bathcontaining 15% sodium chloride at a tem
hed
vagain and dried.
and dried without tension.
’
Example 2
.
-
'
"
Havingnow'particularly described and ascer
perature over 50° C. The ?bers are now was
tained the nature of my said invention, I declare
'
'
that what I claim is.
'
.
1
1; As a new article or manufacture, a ?ber con
Soya bean protein fibers are spun from a solu
tion having the following composition:
sisting of an alkyl-benzene-sulfonic acid salt of
a pseudothiohydantoin, substituted in position 3
Water ___-'__‘____» _________ _-_ ________ __cc'__ 806
by a protein radical selected from the group con- "
Monochloracetic' acid“;______________ __g_,_- 15 10 sisting of phospho-proteins, globulins‘ and prol
arnines, having the formula:
,
Aminoniumthiocyanate___' ____________ __‘g__v 12
p-Toluene sulfonic acid cryst__________ _-g_.. 13
Concentrated ammonium hydroxide_____cc__ 33
Alpha soya bean' protein ___________ _'____g__ 180
After soaking the protein for 30 minutes at a 15
is warmed
temperature of 45° C. the dispersion
to 65° C. and mixed under stirring. The spinning
wherein protein’ represents the-residue of a pro=
tein molecule after removal of NH2—- therefrom.
v solution after permitting to mature is then forced
under stretching through a spinneret into a co
4 2. As a new article of manufacture, a ?ber con
20 sisting of a. para tolu'ene-sulfonic acid salt of a
agulating bath as follows:
pseudothiohydantoin, substituted in position 3 by
Water __'______ ________ __' ________ __per cent__ 55
'
a protein radical selected from the groupof phos
Acid sulfuric -__- _________ .__ _________ _-do___; 25
phoproteins, globulins and prolamines, having the
Sodium sulfate ____.'___1 ______ __'___._do_..__ 20
Temperature _____ _; ________________ __° C_- 45 25
formula:
The ?bers are afterwards thoroughly washed
and dried without tension, using a current of air,
after they were hardened in a bath as follows:
Formaldehyde ___________________________ __
4
protein’
wherein protein’ represents the residue of a -pro
tein molecule after removal of NHz-—- therefrom.
Sodium chloride _-_ _______________________ __
1
3. As a new article of manufacture, a fiber con
i
Per cent
30
Water ____________ __> __________ _‘_ ________ __ 9'5
sisting of a para toluene-sulfonic acid salt of
Example 3
pseudothiohydantoin, substituted in position 3 by
Fibers from zein are prepared by extrusion of 35 the radical of casein, having the formula:
a solution, which isobtainedby dissolving in a
our-s
mixture of 300 cc. of denatured alcohol and 36
cc. of water 1.8 g. monochloracetic acid, 1.35 g.
ammoniu'mthiocyanate and 1.5 g. p-toluene-sul
fonic acid cryst. and after addition of 90 g. of zein 40
casein’
by heating under stirring for a half hour. The
whereincasein'
represents the residue of a casein
spinneret used is the usual forty holes viscose
spinneret and the coagulating bath consists of 5%
aluminum sulfate. After washing the filaments
are stretched in warm water and then passed into
cold water and treated with 6% formaldehyde so
molecule after removal of NH2—- therefrom.
OSKAR HUPPERT.
Документ
Категория
Без категории
Просмотров
0
Размер файла
348 Кб
Теги
1/--страниц
Пожаловаться на содержимое документа